Proteomic Identification of Saliva Proteins as Noninvasive Diagnostic Biomarkers

O’Sullivan, Eleanor; Dowling, Paul; Swandulla, Dieter; Ohlendieck, Kay

doi:10.1007/978-1-0716-2831-7_12

Cited by 5 publications

(6 citation statements)

References 101 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, recent studies that compared the concentration of proteins in saliva and plasma have observed that same components are found in similar concentration in both fluids ( 33 ). Thus, nowadays, saliva is becoming an acceptable diagnostic bio-specimen, mainly due to the advancements in protein analytical techniques ( 34 ). Saliva collection does not require specially trained personnel for sampling procedure, it is easy, non-invasive and more practical ( 32 ).…”

Section: Discussionmentioning

confidence: 99%

“…In the past decades, the most used diagnostic fluids in laboratory setting were blood and urine (32). However, recent studies that compared the concentration of proteins in saliva and plasma have observed that same components are found in similar concentration in both fluids (33). Thus, nowadays, saliva is becoming an acceptable diagnostic bio-specimen, mainly due to the advancements in protein analytical techniques (34).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Salivary cardiac-enriched FHL2-interacting protein is associated with higher diastolic-to-systolic-blood pressure ratio, sedentary time and center of pressure displacement in healthy 7-9 years old school-children

Vasileva,

Font-Lladó,

Carreras-Badosa

et al. 2024

Front. Endocrinol.

View full text Add to dashboard Cite

IntroductionCardiac-enriched FHL2-interacting protein (CEFIP) is a recently identified protein, first found in the z-disc of striated muscles, and related to cardiovascular diseases. Our objectives are: 1) to quantify CEFIP in saliva in healthy 7-9 years old school-children; and 2) to assess the associations of salivary CEFIP concentration and blood pressure, physical (in)activity and physical fitness in these children.MethodsA total of 72 children (7.6 ± 0.3 years) were included in the study, recruited in primary schools in Girona (Spain). A sandwich enzyme-linked immunosorbent assay was used (abx506878; Abbexa, United Kingdom) to quantify CEFIP in saliva. Anthropometric evaluation was performed [body mass, height and body mass index (BMI)]. Systolic and diastolic blood pressure were measured by means of an electronic oscillometer and the diastolic-to-systolic blood pressure ratio (D/S BP ratio) was calculated. Physical (in)activity [sedentary time and time spent in physical activity (PA)] were assessed by means of a triaxial Actigraph GT3X accelerometer (Actigraph, Pensacola, FL, USA) that children were instructed to wear for 24h during 7 conssecutive days. Finally, physical fitness (speed and agility, explosive power of legs, handgrip strength, flexibility and balance) were assessed through validated and standardized testing batteries.ResultsCEFIP was easily detected and measured in all saliva samples (mean concentration: 0.6 ± 0.2 pg/ml). Salivary CEFIP was positively associated with D/S BP ratio (r=0.305, p=0.010) and sedentary time (r=0.317, p=0.012), but negatively associated with PA in 7-9 years old school-children (r=-0.350, p=0.002). Furthermore, salivary CEFIP was related to lower level of balance i.e., higher center of pressure (CoP) displacement in these children (r=0.411, p<0.001). The associations of salivary CEFIP with D/S BP ratio (Beta=0.349, p=0.004), sedentary time (Beta=0.354, p=0.009) and CoP displacement (Beta=0.401, p=0.001), were maintained significant after adjustment for potential confounding variables such as age, gender and BMI in linear regression analyses.ConclusionCEFIP can be easily assessed in saliva as a promising biomarker associated with cardiovascular health in 7-9 years old school-children. Interestingly, higher salivary CEFIP concentration was related to higher D/S BP ratio, more sedentary time and higher CoP displacement i.e., lower level of balance in these children.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Salivary cardiac-enriched FHL2-interacting protein is associated with higher diastolic-to-systolic-blood pressure ratio, sedentary time and center of pressure displacement in healthy 7-9 years old school-children

Vasileva,

Font-Lladó,

Carreras-Badosa

et al. 2024

Front. Endocrinol.

View full text Add to dashboard Cite

show abstract

“…Hence, for the optimum pre-clinical testing of new therapies, the clinical evaluation of diverse patient cohorts during the various phases of clinal studies/trials, and long-term therapeutic monitoring, robust and specific biomarkers for the routine screening of the status of dystrophic patients are required [ 144 , 264 , 265 , 410 , 411 ]. Ideal protein biomarkers would be measurable in a non-invasive, or at least minimally invasive, way and be suitable for repeated sampling procedures [ 325 , 345 , 410 , 411 , 412 ].…”

Section: The Pathoproteomic Profiling Of Duchenne Muscular Dystrophymentioning

confidence: 99%

“…Measurement of the serum carbonic anhydrase isoform CA3 alone versus the ratio of serum myoglobin to CA3 can be used to determine the loss of integrity of dystrophic skeletal muscles versus dystrophin-deficient heart muscle [ 423 ]. An interesting new source of non-invasive biomarkers is represented by the saliva proteome [ 412 ], whose analysis showed elevated levels of the kallikrein isoform Klk1 in the mdx-4cv model of DMD [ 344 , 433 ]. How future multi-omics research initiatives can build on these proteomic findings and establish a more comprehensive pathophysiological picture of dystrophinopathy is briefly outlined in the below section.…”

Section: The Pathoproteomic Profiling Of Duchenne Muscular Dystrophymentioning

confidence: 99%

How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?

Dowling,

Trollet,

Negroni

et al. 2024

Proteomes

Self Cite

View full text Add to dashboard Cite

This perspective article is concerned with the question of how proteomics, which is a core technique of systems biology that is deeply embedded in the multi-omics field of modern bioresearch, can help us better understand the molecular pathogenesis of complex diseases. As an illustrative example of a monogenetic disorder that primarily affects the neuromuscular system but is characterized by a plethora of multi-system pathophysiological alterations, the muscle-wasting disease Duchenne muscular dystrophy was examined. Recent achievements in the field of dystrophinopathy research are described with special reference to the proteome-wide complexity of neuromuscular changes and body-wide alterations/adaptations. Based on a description of the current applications of top-down versus bottom-up proteomic approaches and their technical challenges, future systems biological approaches are outlined. The envisaged holistic and integromic bioanalysis would encompass the integration of diverse omics-type studies including inter- and intra-proteomics as the core disciplines for systematic protein evaluations, with sophisticated biomolecular analyses, including physiology, molecular biology, biochemistry and histochemistry. Integrated proteomic findings promise to be instrumental in improving our detailed knowledge of pathogenic mechanisms and multi-system dysfunction, widening the available biomarker signature of dystrophinopathy for improved diagnostic/prognostic procedures, and advancing the identification of novel therapeutic targets to treat Duchenne muscular dystrophy.

show abstract

“…• Matrisomal proteins: perlecan, biglycan, decorin, alpha-dystroglycan, fibronectin, laminin, mimecan, nidogen, periostin, prolargin, matrix metalloproteinases and a large number of collagen isoforms; In the context of biomarker research, the systematic cataloguing of the skeletal muscle secretome has established that many muscle proteins can be detected in suitable biofluids such as serum/plasma, urine or saliva for diagnostic purposes [324]. Muscle proteins that are associated with the intracellular fractions of myofibers can passively leak or be actively released into the systemic circulation due to strenuous exercise or traumatic muscle damage and then detected in biofluids.…”

mentioning

confidence: 99%

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Dowling,

Swandulla,

Ohlendieck

2023

Cells

Self Cite

View full text Add to dashboard Cite

Voluntary striated muscles are characterized by a highly complex and dynamic proteome that efficiently adapts to changed physiological demands or alters considerably during pathophysiological dysfunction. The skeletal muscle proteome has been extensively studied in relation to myogenesis, fiber type specification, muscle transitions, the effects of physical exercise, disuse atrophy, neuromuscular disorders, muscle co-morbidities and sarcopenia of old age. Since muscle tissue accounts for approximately 40% of body mass in humans, alterations in the skeletal muscle proteome have considerable influence on whole-body physiology. This review outlines the main bioanalytical avenues taken in the proteomic characterization of skeletal muscle tissues, including top-down proteomics focusing on the characterization of intact proteoforms and their post-translational modifications, bottom-up proteomics, which is a peptide-centric method concerned with the large-scale detection of proteins in complex mixtures, and subproteomics that examines the protein composition of distinct subcellular fractions. Mass spectrometric studies over the last two decades have decisively improved our general cell biological understanding of protein diversity and the heterogeneous composition of individual myofibers in skeletal muscles. This detailed proteomic knowledge can now be integrated with findings from other omics-type methodologies to establish a systems biological view of skeletal muscle function.

show abstract

Proteomic Identification of Saliva Proteins as Noninvasive Diagnostic Biomarkers

Cited by 5 publications

References 101 publications

Salivary cardiac-enriched FHL2-interacting protein is associated with higher diastolic-to-systolic-blood pressure ratio, sedentary time and center of pressure displacement in healthy 7-9 years old school-children

Salivary cardiac-enriched FHL2-interacting protein is associated with higher diastolic-to-systolic-blood pressure ratio, sedentary time and center of pressure displacement in healthy 7-9 years old school-children

How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Contact Info

Product

Resources

About