Lactadherin
Lactadherin, also known asMFG-E8(Milk Fat Globule-Epidermal Growth Factor 8), is a glycoprotein found in various bodily fluids, including plasma, milk, and cerebrospinal fluid. It plays a crucial role in several physiological processes due to its unique ability to bind to phosphatidylserine, a lipid typically exposed on the surface of apoptotic (dying) cells. This binding facilitates the recognition and clearance of these cells by phagocytes, a process essential for maintaining tissue homeostasis and preventing inflammation. Beyond its role in apoptotic cell clearance, lactadherin is also involved in cell adhesion, immune response modulation, and tissue remodeling.
Biological Basis
Section titled “Biological Basis”The biological function of lactadherin is primarily mediated by its two key domains: an epidermal growth factor (EGF)-like domain and two factor VIII-like (C1/C2) domains. The EGF-like domain contains an RGD (Arg-Gly-Asp) motif, which allows it to interact with integrins on the surface of various cells, promoting cell adhesion and signaling. The C1/C2 domains are responsible for binding to phosphatidylserine, acting as a bridge between apoptotic cells and phagocytes. This dual functionality enables lactadherin to modulate cellular interactions and immune responses in diverse contexts.
Clinical Relevance
Section titled “Clinical Relevance”Measuring the levels of lactadherin in plasma and other biological samples has gained attention for its potential clinical utility. Like other plasma proteins, lactadherin levels are influenced by genetic factors, known as protein quantitative trait loci (pQTLs). Studies analyzing the whole-genome sequence and the plasma proteome aim to identify these pQTLs and connect genetic risk to disease endpoints, such as cardiovascular disease.[1]Understanding the genetic architecture of plasma proteins can provide insights into disease mechanisms and help identify potential biomarkers.
Social Importance
Section titled “Social Importance”The study of lactadherin and its genetic determinants holds significant social importance. By identifying genetic variants that affect lactadherin levels, researchers can better understand individual predispositions to various health conditions. This knowledge could lead to the development of more precise diagnostic tools and personalized therapeutic strategies. For example, if specific genetic profiles are associated with altered lactadherin levels and increased disease risk, interventions could be tailored to individuals based on their genetic makeup. Moreover, lactadherin’s role in fundamental biological processes means that insights gained from its study could have broader implications for understanding and treating a wide array of human diseases, ultimately contributing to improved public health outcomes.
Methodological and Statistical Considerations
Section titled “Methodological and Statistical Considerations”Research into lactadherin often faces limitations stemming from study design and statistical power. Many genomic association studies, while powerful, are observational, meaning they cannot definitively establish causality between genetic variants and lactadherin levels but rather identify associations.[2]The ability to detect genetic variants with smaller effects on lactadherin levels is also constrained by current sample sizes, as polygenic scores for protein traits are primarily driven by variants with larger effects.[3] Furthermore, the choice of statistical methods for genome-wide association studies (GWAS) can influence replication rates and the identification of independent loci, potentially leading to varied results across different analytical approaches.[4] The calibration and robustness of statistical models are crucial for reliable interpretation. While some methods demonstrate good calibration, particularly for low-prevalence traits or in homogeneous populations, their performance can vary.[4] For instance, certain mixed-model methods may produce inflated test statistics in datasets with high levels of relatedness or non-homogeneous ancestry, impacting the accuracy of false-positive rate estimates and potentially leading to spurious associations.[4]These statistical nuances highlight the need for careful method selection and validation to ensure the integrity of findings related to lactadherin.
Population Diversity and Generalizability
Section titled “Population Diversity and Generalizability”A significant limitation in understanding lactadherin genetics is the predominant focus on populations of European ancestry in many large-scale studies. For example, some GWAS analyses for plasma protein traits have primarily utilized European participants from cohorts like the UK Biobank.[4] This bias can lead to results that are not fully generalizable to other populations, as genetic architectures and allele frequencies can differ substantially across diverse ancestries.[3] The underrepresentation of non-European populations can also introduce biases in genetic analyses, such as those related to imputation panels, potentially favoring European-specific variants.[3] While efforts are made to mitigate these issues, such as using whole-genome sequencing (WGS) data to ensure high-quality variant information across different ancestries, population-specific variants might still be overlooked if not present in all analyzed cohorts.[3]Consequently, insights into lactadherin’s genetic determinants might be incomplete, and findings may not fully translate to individuals of non-European descent.
Phenotypic Complexity and Unaccounted Factors
Section titled “Phenotypic Complexity and Unaccounted Factors”The and interpretation of plasma lactadherin levels are subject to considerable phenotypic complexity and potential confounding factors. Raw protein measurements undergo extensive preprocessing, including log transformation, scaling, residualization for covariates like age, sex, and ancestry principal components, and inverse normalization.[1]While these steps aim to standardize data and account for known confounders, the resulting phenotype is highly adjusted, which may complicate the direct biological interpretation of raw lactadherin levels and their associated genetic effects.
Beyond genetic factors, a range of environmental and lifestyle confounders can influence lactadherin levels, including diet, alcohol consumption, smoking status, body mass index, and overall health.[4] Although studies often adjust for numerous covariates, residual confounding by unmeasured or imperfectly measured environmental factors, or complex gene-environment interactions, can still exist. Moreover, for some proteins, a substantial portion of heritability remains unexplained, indicating that current genetic models may not fully capture all contributing genetic variants, or that non-genetic factors play a more dominant role.[1]
Variants
Section titled “Variants”Genetic variations play a crucial role in influencing the levels and functions of various proteins, including lactadherin. Variants in theMFGE8gene, which encodes lactadherin (also known as milk fat globule-EGF factor 8 protein), directly impact its expression and activity, affecting processes like the clearance of apoptotic cells, immune modulation, and tissue remodeling. Specific single nucleotide polymorphisms (SNPs) such asrs34239095 , rs12909463 , and rs111672988 within or near MFGE8can alter lactadherin levels or its binding affinity, which is critical for its biological roles. Additionally, variants in the intergenic region betweenMFGE8 and KRT18P47, including rs117217783 , rs143253594 , and rs1961839 , may regulate MFGE8expression or other nearby genes that indirectly affect lactadherin pathways. These genetic associations with intermediate traits like protein levels are often stronger than with disease endpoints, highlighting their importance in understanding underlying biological mechanisms.[5] Such pQTLs (protein quantitative trait loci) can explain a significant portion of the variance in plasma protein concentrations, providing insights into potential causal genes.[6]Other variants in genes involved in immune responses and cellular maintenance also contribute to the complex network influencing lactadherin-related processes. TheMS4A6A gene, with its variant rs7232 , and MS4A4A with rs7117320 , belong to the membrane-spanning 4A gene family, known for their roles in immune cell signaling and inflammation. Changes in these genes could modulate the inflammatory environment or immune cell function, indirectly affecting lactadherin’s involvement in immune regulation. Similarly, the intergenic variantrs189448562 between SIGLEC1 and HSPA12B is relevant, as SIGLEC1 (sialic acid-binding Ig-like lectin 1) is a macrophage receptor important for immune recognition, and HSPA12B(heat shock protein family A member 12B) is involved in stress responses and inflammation. These variants highlight how genetic factors can influence immune and stress pathways that often intersect with lactadherin’s functions. Studies have shown that genetic variants can determine levels of various plasma proteins, including those involved in immune processes.[1]Further genetic influences on lactadherin pathways come from genes with broader regulatory and metabolic roles. TheNCOR2 gene, associated with rs2141247 , encodes a nuclear receptor corepressor that modulates gene expression, thereby having widespread effects on cellular processes, including metabolism and inflammation. Similarly, the GCKR gene, linked to rs1260326 , regulates glucokinase activity and is a key player in glucose and lipid metabolism; variants here are often associated with metabolic traits like triglyceride levels. Given lactadherin’s emerging links to metabolic health,GCKR variants could be particularly relevant. The SLC44A4 gene (rs521977 ) encodes a choline transporter crucial for cell membrane integrity and signaling, while ZPR1 (rs964184 ) is involved in cell proliferation and ribosome biogenesis. These genes, through their fundamental cellular roles, can influence the overall physiological context in which lactadherin functions, potentially impacting its circulating levels or efficacy in various biological processes. Identifying specific trans-pQTLs can reveal biologically meaningful interactions between genetic variants and protein levels.[6]
Key Variants
Section titled “Key Variants”| RS ID | Gene | Related Traits |
|---|---|---|
| rs7232 | MS4A6A | late-onset Alzheimers disease circulating fibrinogen levels soluble triggering receptor expressed on myeloid cells 2 blood protein amount apolipoprotein D |
| rs34239095 rs12909463 rs111672988 | MFGE8 | alkaline phosphatase lactadherin |
| rs964184 | ZPR1 | very long-chain saturated fatty acid coronary artery calcification vitamin K total cholesterol triglyceride |
| rs7117320 | MS4A4A | lactadherin |
| rs56405824 rs114940034 | KRT18P47 - CARMAL | lactadherin eye colour |
| rs117217783 rs143253594 rs1961839 | MFGE8 - KRT18P47 | lactadherin |
| rs189448562 | SIGLEC1 - HSPA12B | level of G-protein coupled receptor family C group 5 member C in blood lactadherin level of angiopoietin-related protein 2 in blood CD63 antigen level of Na(+)/H(+) exchange regulatory cofactor NHE-RF2 in blood |
| rs2141247 | NCOR2 | lactadherin platelet component distribution width total cholesterol , blood VLDL cholesterol amount level of receptor-type tyrosine-protein phosphatase beta in blood |
| rs1260326 | GCKR | urate total blood protein serum albumin amount coronary artery calcification lipid |
| rs521977 | SLC44A4 | BMI-adjusted waist-hip ratio mosquito bite reaction itch intensity perceived unattractiveness to mosquitos mosquito bite reaction itch intensity , mosquito bite reaction size lactadherin |
The Dynamic Plasma Proteome and its Molecular Functions
Section titled “The Dynamic Plasma Proteome and its Molecular Functions”The human plasma proteome represents a vast and dynamic collection of proteins and protein complexes circulating throughout the body, playing critical roles in maintaining physiological homeostasis and mediating various biological processes. These proteins encompass a wide range of molecular functions, including those involved in signaling pathways, metabolic regulation, and cellular interactions.[7] Advanced proteomic technologies, such as aptamer-based assays, enable the of thousands of these plasma proteins, including both extracellular and intracellular components, as well as soluble domains of membrane-associated proteins, with a particular focus on those secreted into the bloodstream.[7]The diverse nature of these circulating biomolecules, which include critical proteins, enzymes, receptors, and hormones, underscores their importance as indicators of systemic health and disease.
Many plasma proteins are integral to complex regulatory networks and cellular functions. For instance, the receptor tyrosine kinase TIE1 plays a role in upregulating adhesion molecules in endothelial cells, impacting vascular biology.[8] Similarly, the Notch/CBF-1 signaling pathway is regulated by mechanical forces like cyclic strain in endothelial cells, influencing angiogenic activity and vascular development.[9] Other key molecules like vascular endothelial growth factor (VEGF) can induce interactions between proteins such as Shc and vascular endothelial cadherin, suggesting feedback mechanisms in VEGFR2 signaling, while VEGFR2 and VEGFR3 can form heterodimers on angiogenic sprouts, highlighting their involvement in blood vessel formation.[10] Glycosylation, a common post-translational modification, also influences protein function, as seen in the complement system’s interactions with glycans and the binding of mannan-binding lectin to α2 macroglobulin via oligomannose glycans.[11]
Genetic Regulation of Circulating Protein Levels
Section titled “Genetic Regulation of Circulating Protein Levels”Genetic mechanisms exert a significant influence on the circulating levels of plasma proteins, a phenomenon widely studied through protein quantitative trait loci (pQTLs). These pQTLs identify specific genetic variants that are associated with variations in protein concentrations in the blood.[5] The genetic architecture of plasma proteins can be broadly categorized by cis-pQTLs, where genetic variation near the gene encoding the protein explains a substantial portion of its plasma concentration, and trans-pQTLs, where the genetic influence originates from distant genomic regions, often affecting entire pathways or exhibiting more general effects.[6] For example, some protein levels, such as those of Haemopexin (HPX) and SLAMF7, can be determined by multiple independent genetic variants.[5]Genetic variations can impact protein levels through various mechanisms. A genetic variant within a protein-coding sequence, known as a protein-altering variant (PAV), can directly affect the protein’s higher-order structure or its binding affinity to other molecules, including aptamers used in assays.[6] Such PAVs are often responsible for strong and isolated genetic effects on protein concentrations.[6] Beyond direct structural changes, genetic regulatory elements can influence gene expression patterns, leading to altered protein production. The identification of allele-specific transcription co-associated with expression quantitative trait loci (eQTLs) can help distinguish between structural and regulatory genetic effects, further enhancing the understanding of how genetic variants control the proteome.[5]
Proteomic Insights into Pathophysiological Processes
Section titled “Proteomic Insights into Pathophysiological Processes”The plasma proteome serves as a critical bridge connecting genetic risk factors to disease endpoints, offering a window into pathophysiological processes and homeostatic disruptions.[5] Many circulating proteins are known to be involved in the development and progression of human diseases, making them valuable biomarkers and potential therapeutic targets.[7]For instance, the levels of tumor markers like CA19-9 and DU-PAN-2 in colorectal cancer patients are influenced by Lewis and secretor gene dosages, demonstrating how genetic background can affect disease-related biomolecule concentrations.[12] Beyond oncology, proteomic studies provide insights into various conditions, including inflammatory and metabolic disorders. For example, polymorphisms in mannan-binding lectin (MBL) have been linked to rheumatoid arthritis, highlighting the role of immune system components in autoimmune diseases.[13]Furthermore, analysis of the plasma proteome has yielded novel insights into cardiovascular disease, underscoring the systemic impact of protein alterations.[1] The study of plasma proteins also extends to metabolic health, with markers like 1,5-Anhydroglucitol serving as non-invasive indicators of short-term glycemic control.[14] A comprehensive understanding of the genetic control over these circulating protein drug targets and biomarkers is essential for improving pharmaceutical interventions and the design of clinical trials.[5]
Systemic Consequences and Tissue Interactions
Section titled “Systemic Consequences and Tissue Interactions”Plasma proteins are integral to tissue and organ-level biology, reflecting systemic consequences and complex tissue interactions across the body. The proteins circulating in plasma originate from various tissues and organs, acting as messengers and mediators in a wide array of physiological processes. The of these proteins, including those biased towards the human secretome, provides a broad perspective on the body’s internal state.[7] For example, proteins like TIE1 and components of the Notch signaling pathway are critical in endothelial cells, suggesting their involvement in the health and function of the vascular system.[8]The systemic nature of the plasma proteome means that disruptions or changes in protein levels can have far-reaching effects, influencing multiple organ systems. This is evident in diseases like rheumatoid arthritis, which has systemic inflammatory consequences, and cardiovascular disease, which impacts the heart and circulatory system.[1]The interconnectedness of biological processes is further highlighted by studies showing that genetic variants can influence protein levels that, in turn, affect various disease endpoints, illustrating a proteo-genomic convergence in human diseases.[6]Understanding these systemic interactions and organ-specific effects through plasma proteomics is crucial for unraveling the complexity of human health and disease.
Genetic Control of Plasma Protein Levels
Section titled “Genetic Control of Plasma Protein Levels”The abundance of circulating proteins in human plasma is under significant genetic control, with specific genetic variants influencing protein expression and stability. These genetic determinants, known as protein quantitative trait loci (pQTLs), can be categorized as cis-pQTLs, located near the gene encoding the protein, or trans-pQTLs, affecting proteins encoded on different chromosomes.[6] Trans-pQTLs are particularly noteworthy as they can explain a substantial portion of the variance in plasma protein levels, indicating complex regulatory networks where a single genetic variant can impact multiple proteins.[5] This intricate genetic architecture often converges with regulatory mechanisms governing gene expression and splicing, suggesting that genetic variants influence protein abundance through multi-layered transcriptional and post-transcriptional controls.[6] Further illustrating this genetic influence, specific gene dosages, such as those of the Lewis and secretor genes, directly affect the serum concentrations of certain glycoproteins like CA19-9 and DU-PAN-2.[12]This demonstrates how genetic predispositions can dictate the baseline levels and modifications of plasma proteins. Understanding these foundational genetic controls is crucial for interpreting variations in circulating protein measurements and their potential links to health and disease.[5]
Signaling and Receptor-Mediated Regulation
Section titled “Signaling and Receptor-Mediated Regulation”The regulation of circulating protein levels is intimately connected to a variety of signaling pathways that orchestrate cellular functions and systemic homeostasis. Receptor activation, particularly involving receptor tyrosine kinases such as soluble Tie-1 or VEGF receptor 2/3, plays a key role in influencing the abundance and activity of proteins involved in vascular biology and angiogenesis.[8] For instance, VEGF stimulation can induce the association of Shc with vascular endothelial cadherin, establishing a feedback mechanism that modulates VEGF receptor-2 signaling and consequently impacts protein dynamics within the vasculature.[15] Intracellular signaling cascades, including the Notch/CBF-1 pathway, are also critical regulators. Cyclic mechanical strain, for example, has been shown to regulate the Notch/CBF-1 pathway in endothelial cells, influencing their angiogenic activity and the expression of related proteins like NOTCH1.[9] The levels of key signaling components, such as the Insulin receptor, are themselves subject to genetic control, highlighting how genetic variation can propagate through signaling pathways to affect overall protein profiles.[5]
Metabolic Pathways and Protein Function
Section titled “Metabolic Pathways and Protein Function”Proteins are integral to numerous metabolic pathways, participating in energy metabolism, biosynthesis, and catabolism, with genetic variations significantly influencing these processes. A genome-wide perspective reveals extensive genetic variation impacting human metabolism, demonstrating a broad influence on metabolic traits.[16] For example, specific gene loci like SULT2A1, which is involved in the metabolism of sulfated steroids and primary bile acids, illustrate how genetic variants can alter enzyme activity and subsequent metabolite concentrations.[6] Such alterations can lead to profound physiological consequences, as seen with the concurrent inverse association of SULT2A1 activity with lower plasma concentrations of secondary bile acids like glycholithocholate, potentially promoting cholesterol crystallization and gallstone formation.[6] This intricate interplay between protein levels and metabolic flux underscores how proteins contribute to both metabolic regulation and the emergent properties of biological systems, influencing overall metabolic health.
Post-Translational Modification and Protein Dynamics
Section titled “Post-Translational Modification and Protein Dynamics”Beyond direct genetic regulation of their synthesis, the functional properties and circulating concentrations of proteins are profoundly influenced by post-translational modifications. Glycosylation, a common modification, is critical for protein stability, function, and interactions, particularly with components of the complement system.[17] For example, the interaction between mannan-binding lectin and alpha-2 macroglobulin mediated by exposed oligomannose glycans demonstrates how these modifications dictate complex protein-protein interactions and biological processes.[11]Furthermore, genetic variations can impact a protein’s higher-order structure, which in turn affects its binding affinity and overall function, a phenomenon detectable by aptamer-based techniques.[5] The existence of functionally distinct protein alleles, such as those encoded by ERAP1 haplotypes that exhibit fine substrate specificity, illustrates how subtle genetic differences can lead to significant functional variations in protein activity and dynamic interactions within the body.[5]
Systems-Level Integration and Disease Pathogenesis
Section titled “Systems-Level Integration and Disease Pathogenesis”The regulation of plasma protein levels occurs within a highly integrated biological system characterized by extensive pathway crosstalk and complex network interactions. Protein quantitative trait loci (pQTLs) frequently overlap with genetic risk loci identified in disease-genome-wide association studies (GWAS), establishing critical links between specific proteins and the pathogenesis of complex disorders.[5]For example, the extracellular matrix glycoproteinFBLN3 (encoded by EFEMP1) is connected to a large number of diseases and phenotypes, highlighting its role as a central node in various disease networks.[6]Dysregulation within these intricate protein networks can directly contribute to disease, as evidenced by theFTOobesity variant circuitry impacting adipocyte browning.[18] or complement activation by heme acting as a secondary hit in atypical hemolytic uremic syndrome.[19] Understanding these systems-level interactions not only sheds light on compensatory mechanisms but also facilitates the identification of novel therapeutic targets, where aptamer-based proteomic profiling can serve as an intermediate trait for drug-target validation and identifying differential responders to therapeutic interventions.[5]
Prognostic Value and Risk Stratification
Section titled “Prognostic Value and Risk Stratification”The study of plasma protein levels, such as lactadherin, offers significant prognostic potential by elucidating the genetic underpinnings of circulating protein abundance and its link to disease outcomes. Genetic variants that influence plasma protein levels, known as protein quantitative trait loci (pQTLs), can serve as robust predictors of disease progression and long-term implications.[1]For instance, in cardiovascular disease, analyzing the plasma proteome in diverse populations, including Black adults, provides novel insights into disease pathways and can help identify high-risk individuals.[1]This approach enables more personalized medicine strategies, allowing for the identification of individuals at elevated risk for specific conditions and facilitating targeted prevention strategies before overt disease manifestation.[2]
Diagnostic Applications and Therapeutic Guidance
Section titled “Diagnostic Applications and Therapeutic Guidance”Lactadherin, as a plasma protein, holds promise as a diagnostic biomarker, with its levels potentially reflecting various physiological and pathological states. Understanding the genetic control over circulating protein levels can significantly improve the selection of pharmaceutical interventions and the design of clinical trials.[5] For example, specific aptamers developed to bind proteins can be readily adapted into precise clinical assays, potentially identifying individuals who would respond differentially to immunotherapies or other treatments.[5]The reliability of protein measurements, as demonstrated by platforms like SOMAscan and Olink, supports their utility in clinical settings for monitoring disease activity or treatment efficacy, ensuring that robust associations can be translated into practical patient care.[2]
Elucidating Disease Mechanisms and Comorbidities
Section titled “Elucidating Disease Mechanisms and Comorbidities”Analysis of plasma proteins, including lactadherin, plays a crucial role in mapping the complex interplay between genetic risk and disease endpoints, thereby enhancing our understanding of disease mechanisms and associated comorbidities. By connecting genetic variants to protein levels and then to clinical phenotypes, researchers can uncover underlying biological pathways, identify related conditions, and recognize overlapping disease presentations.[6]This proteo-genomic convergence is vital for discovering new biomarkers and disease pathways, especially when extended to diverse populations, which can reveal unique genetic architectures and clinical associations that might otherwise be missed.[1]Such comprehensive insights contribute to a more holistic understanding of human health and disease, informing future therapeutic development and patient management.
Frequently Asked Questions About Lactadherin
Section titled “Frequently Asked Questions About Lactadherin”These questions address the most important and specific aspects of lactadherin based on current genetic research.
1. Why do some people seem healthier than me, even with similar habits?
Section titled “1. Why do some people seem healthier than me, even with similar habits?”Genetic differences play a big role in individual health. Your body’s ability to clear old cells, partly managed by proteins like lactadherin, can be genetically influenced. This means some people might have a natural advantage in maintaining tissue health, even with similar lifestyles. Understanding these genetic variations could help explain such differences.
2. Does my diet affect my body’s ‘clean-up crew’ like old cells?
Section titled “2. Does my diet affect my body’s ‘clean-up crew’ like old cells?”Yes, what you eat can indirectly influence your body’s cellular clean-up processes. Lactadherin, crucial for clearing dying cells, can have its levels affected by lifestyle factors like diet. While more research is needed to pinpoint exact dietary impacts, maintaining a healthy diet supports overall bodily functions, including this vital cell clearance.
3. My family has heart problems; am I more at risk too?
Section titled “3. My family has heart problems; am I more at risk too?”Yes, there’s a good chance your family history impacts your risk. Genetic factors that influence your lactadherin levels, a protein involved in clearing old cells and immune responses, are known to connect to conditions like cardiovascular disease. Understanding these inherited predispositions can help you take proactive steps for your heart health.
4. Can a special blood test tell me about my future health risks?
Section titled “4. Can a special blood test tell me about my future health risks?”Potentially, yes. Measuring proteins like lactadherin in your blood is gaining attention for its ability to reveal insights into your health. Since lactadherin levels are linked to genetic factors and disease risks, a specific test could help identify individual predispositions to certain conditions, guiding more personalized health strategies.
5. Does my ancestry affect my specific health challenges?
Section titled “5. Does my ancestry affect my specific health challenges?”Yes, your genetic ancestry can play a role in your unique health profile. Many genetic studies, including those on proteins like lactadherin, have primarily focused on people of European descent. This means genetic risk factors and their impact might be different or less understood for other ancestries, highlighting the need for more diverse research.
6. Is it true that stress can impact my body’s internal repair?
Section titled “6. Is it true that stress can impact my body’s internal repair?”While direct links between stress and lactadherin levels are still being explored, stress is a significant factor in overall health. Your body’s internal repair processes, including the vital clearance of dying cells facilitated by lactadherin, are sensitive to your general well-being. Managing stress can contribute to supporting these crucial bodily functions.
7. Why do some people never seem to get sick, unlike me?
Section titled “7. Why do some people never seem to get sick, unlike me?”Individual differences in immune response, partly influenced by genetics, could be a factor. Proteins like lactadherin play a role in modulating your immune system and clearing unwanted cells. Genetic variations can affect how efficiently these processes work, potentially leading to different susceptibilities to illness among individuals.
8. Can exercise help overcome my family’s health history?
Section titled “8. Can exercise help overcome my family’s health history?”Exercise is a powerful tool, even with a strong family health history. While genetic factors influencing proteins like lactadherin can predispose you to certain conditions, lifestyle choices such as regular exercise can positively influence your overall health and potentially mitigate some genetic risks. It’s a key part of a personalized strategy to stay healthier.
9. Does my age affect how well my body cleans itself internally?
Section titled “9. Does my age affect how well my body cleans itself internally?”Yes, your age is a known factor that influences many bodily processes, including how efficiently your body clears old or dying cells. Levels of proteins like lactadherin, which are crucial for this internal clean-up, can change as you get older. Researchers often account for age when studying these proteins to understand specific health impacts.
10. Could knowing my genetics help me choose better medicines?
Section titled “10. Could knowing my genetics help me choose better medicines?”Absolutely, understanding your genetics is a key step towards personalized medicine. If specific genetic profiles are linked to altered lactadherin levels and disease risk, knowing your genetic makeup could help doctors tailor treatments or preventive strategies specifically for you, potentially leading to more effective and safer therapies.
This FAQ was automatically generated based on current genetic research and may be updated as new information becomes available.
Disclaimer: This information is for educational purposes only and should not be used as a substitute for professional medical advice. Always consult with a healthcare provider for personalized medical guidance.
References
Section titled “References”[1] Katz, D. H. et al. “Whole Genome Sequence Analysis of the Plasma Proteome in Black Adults Provides Novel Insights Into Cardiovascular Disease.”Circulation, 2021.
[2] Dhindsa, R. S. et al. “Rare variant associations with plasma protein levels in the UK Biobank.” Nature, 2023.
[3] Thareja, G. et al. “Differences and commonalities in the genetic architecture of protein quantitative trait loci in European and Arab populations.” Hum Mol Genet, 2022.
[4] Loya, H. “A scalable variational inference approach for increased mixed-model association power.” Nature Genetics, vol. 57, no. 2, 2025, pp. 461–468.
[5] Suhre, K. et al. “Connecting genetic risk to disease end points through the human blood plasma proteome.”Nat Commun, 2017.
[6] Pietzner, M. et al. “Mapping the proteo-genomic convergence of human diseases.” Science, 2021.
[7] Sun, B. B. et al. “Genomic atlas of the human plasma proteome.” Nature, 2018.
[8] Chan, B. et al. “Receptor tyrosine kinase Tie-1 overexpression in endothelial cells upregulates adhesion molecules.” Biochem. Biophys. Res. Commun., vol. 371, 2008, pp. 475–479.
[9] Morrow, D. et al. “Cyclic strain regulates the Notch/CBF-1 signaling pathway in endothelial cells: Role in angiogenic activity.” Arterioscler. Thromb. Vasc. Biol., vol. 27, 2007, pp. 1289–1296.
[10] Nilsson, I. et al. “VEGF receptor 2/-3 heterodimers detected in situ by proximity ligation on angiogenic sprouts.” EMBO J., vol. 29, 2010, pp. 1377–1388.
[11] Arnold, J. N. et al. “Interaction of mannan binding lectin with α2 macroglobulin via exposed oligomannose glycans: a conserved feature of the thiol ester protein family?” J. Biol. Chem., vol. 281, 2006, pp. 6955–6963.
[12] Narimatsu, H. et al. “Lewis and secretor gene dosages affect CA19-9 and DU-PAN-2 serum levels in normal individuals and colorectal cancer patients lewis and secretor gene dosages affect CA19-9 and DU-PAN-2 serum levels in normal individuals and colorectal cancer patients1.”Cancer Res., vol. 58, no. 3, 1998, pp. 512–518.
[13] Song, G. G. et al. “Meta-analysis of functional MBL polymorphisms.” Z. Rheumatol., vol. 73, 2014, pp. 657–664.
[14] Mook-Kanamori, D. O. et al. “1,5-Anhydroglucitol in saliva is a noninvasive marker of short-term glycemic control.” J. Clin. Endocrinol. Metab., vol. 99, 2014, pp. E479–E483.
[15] Zanetti, A. et al. “Vascular endothelial growth factor induces Shc association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling.” Arterioscler. Thromb. Vasc. Biol., vol. 22, 2002, pp. 617–622.
[16] Illig, T. et al. “A genome-wide perspective of genetic variation in human metabolism.” Nat. Genet., vol. 42, no. 2, 2010, pp. 137–141.
[17] Ritchie, G. E. et al. “Glycosylation and the complement system.” Chem. Rev., vol. 102, 2002, pp. 305–319.
[18] Claussnitzer, M. et al. “FTO obesity variant circuitry and adipocyte browning in humans.”N. Engl. J. Med., vol. 373, no. 10, 2015, pp. 895–907.
[19] Frimat, M. et al. “Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome.” Blood, vol. 122, no. 3, 2013, pp. 282–292.