Histological and morphometric analysis of skeletal muscle in some vertebrates
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Abstract
The skeletal system is primarily driven by the skeletal muscles to produce kinematic movements. The study evaluates the histological and morphometric properties of skeletal muscle in Clarias gariepenus (Cl. gariepinus), Bufo bufo (B. bufo), Agama agama (A. agama), Columba livia domestica (C. domestica) and Rattus rattus (R. rattus). The study was carried in order to relate the similarities anddifferences of skeletal muscles in these species with evolutionary trend. The epaxial muscle of Cl. Gariepinus, the biceps femoris muscle of B. bufo, R. rattus, puboischiotibialis of A. agama, and pectoralmuscle from C. domestica were removed and assessed grossly for physical appearance then processed for histological analysis. The diameters of the muscle fibers were measured and one-way analysis of variance was used to compare the differences. The muscles of Cl. gariepinus, B. bufo and agama appeared whitish with scanty fusiform nucleus and large intermuscular space. However, the muscles of C. domestica and R. rattus appeared red with distinct round nucleus and small intermuscular space. No significant difference (P>0.05) was observed in the muscle diameter of Cl. gariepinus (8.86±0.13µm) compared to B. bufo (8.25±0.27µm). The muscle diameter of A. agama (10.18±0.25µm) was significantly higher (P<0.05) relative to Cl. gariepinus (8.86±0.13µm), B. bufo (8.25±0.27µm), C. domestica (3.38±0.13µm) and R. rattus (4.66±0.15µm). Conclusively, non-tetrapod vertebrates (Cl. gariepinus, B. bufo, and A. agama) have simple, white-colored skeletal muscle with few flat-shaped nuclei and large fiber diameters while higher vertebrates (C. domestica and R. rattus) have complex, red-colored skeletal muscle with numerous oval-shaped nucleus and small fiber diameter.
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References
Buehler, C., Koller, W., De Comtes, F. and Kainz, H. (2021). Quantifying muscle forces and joint loading during hip exercise perform with and without an elastic Resistance Band. Frontiers in Sports and Active Living, 3(695383): 1-13.
Conlon, J.M. (2013). Evolution in action: Skin Peptides. In: Kastin AJ, (eds) Handbook of biologically active peptides. Academic Press, pp 1842-
Csapo, R., Gumpenberger, M. and Wessner, B. (2020). Skeletal muscle extracellular matrix - what do we know about its composition, regulation, and physiological roles? A narrative review. Frontiers in Physiology, 11(253): 1-14.
Dauncey, M.J. and Ingram, D.L. (1988). Influenced of environmental temperature and energy Intake on skeletal muscle respiratory enzymes
and morphology. European Journal of Applied Physiology, 58: 239-244.
Donoghue, P.C.J. and Purnell, M.A. (2009). The evolutionary emergence of vertebrates from among their spineless relatives. Evolution: Education and Outreach. 2: 204-212.
Elanga, J., Hou, C., Bao, B., Wang, S., Maté Sánchez de Val, J.E. and Wenhui, W. (2022). The molecular interaction of collagen with cell receptors for biological function. Polymers, 14(5): 876.
Portner, H-O. (2011). Cellular Energy Utilization: Environmental Influences on Metabolism. In: Farrell, A. P. (ed.) Encyclopedia of fish physiology: from genome to environment. Academic Press Elsevier, Montpellier, pp 1645-1651.
Faroni, A., Smith, R.J. and Reid, A.J. (2014). Adipose-derived stem cells and nerve regeneration. Neural Regeneration Research, 9: 1341-1346.
Gamblin, D.P., Scanlan, E.M. and Davis, B.G. (2009). Glycoprotein synthesis: An update. Chemical Reviews, 109: 131-163.
Gemballa, S., Ebmeyer, L., Hagen, K., Hannich, T., Hoja, K., Rolf, M. and Weitbrecht, G. (2003). Evolutionary transformations of myoseptal tendons in gnathostomes. Proceedings of the Royal Society B: Biological Sciences, 270: 1229-1235.
Gillies, A.R. and Lieber, R.L. (2011). Structure and function of the skeletal muscle extracellular matrix. Muscle Nerve,44(3): 318-331.
Granic, A., Sayer, A.A. and Robinson, S.M. (2019). Dietary pattern, skeletal muscles health, and sarcopenia in older adults. Nutrients, 11: 745.
Halper, J. and Kjaer, M. (2014). Basic components of connective tissues and extracellular matrix: elastin, fibrillin,fibulins, fibrinogen, fibronectin, laminin, tenascins, and thrombospondins. Advances in Experimental Medicine and Biology, 802: 31-47.
Heymsfield, S.B., Stanley, A., Pietrobelli, A. and Heo, M. (2020). Simple skeletal muscle mass estimation formulas: What we can learn from them? Frontiers in Endocrinology, 11(31): 1-5.
Holeček, M. and Mičuda, S. (2017). Amino acid concentrations and protein metabolism of two types of rat skeletal muscle in
postprandial state and after brief starvation. Physiology Research, 66: 959-967.
Ishaya, P., Attah, M.O.O., Dibal, N.I. and Chiroma, M.S. (2022). Histomorphological and morphometric analysis of the tongue in the Agama
lizard (Agama Agama), toad (Bufo Bufo) and rabbit (Oryctolagus Cuniculus Domesticus). Journal of Morphological Sciences, 39: 88-94.
Janssen, I., Steven, B., Wang, H.Z. and Robert, R. (2000). Skeletal muscle mass and distribution in 468 men and women aged 18–88 yr. Journal of Applied Physiology, 89: 81-88.
Jones, K.E., Angielczyk, K.D. and Pierce, S.E. (2019). Stepwise shifts underlie evolutionary trends in morphological complexity of the mammalian vertebral column. Nature Communications, 10(5071): 1-13
Karagounis, L.G. and Hawley, J.A. (2010). Skeletal muscle: Increasing the size of the locomotor cell. The International Journal of Biochemistry and Cell Biology, 42: 1376-1379.
Kardong, K.V. (2012). Verebrates comparative anatomy, function, evolution. 6th Edition, McGraw-Hill, New York.
Kristensen, J.H. and Karsdal, M.A. (2016). Elastin. In: Karsdal MA (eds) biochemistry of collagens, laminins, and elastin: structure, function, and biomarkers. Odense; Academic Press.
Lelievre P.G. and Oldenburg, D.W. (2009). A comprehensive study of including structural orientation information in geophysical inversions. Geophysical Journal International, 178: 623-637.
Luna, V.M., Daikoku, E. and Ono, F. (2015). “Slow” skeletal muscle across vertebrate species. Cell Bioscience, 5: 62.
Mahrous, K.F., Mabrouk, D.M., Aboelenin, M.M., Abd El kader, H.A.M. and Hassanane, M.S. (2021). Identification and characterization of antimicrobial peptide genes in Clarias gariepinus and Chelon ramada. Jordan Journal of Biological Sciences, 14: 51-64.
Martínez, M.A.R., Galisteo, S.P., Castán, H. and Hernández, M.E.M. (2020). Role of proteoglycans on skin ageing: a review. International Journal of Cosmetic Science, 42: 529-535.
Mengeste, A.M., Rustan, A.C. and Lund, J. (2021). Skeletal muscle energy metabolism in obesity. Obesity (Silver Spring), 29:1582–1595.
Meyers, R.A. and McFarland, J.C. (2016). Anatomy and histochemistry of spreadwing pasture in birds. 4. Eagles soar with fast, not slow muscle fibers. Acta Zoology, 97: 319-324.
Meyers, R.A. and Stakebake, E.F. (2005). Anatomy and histochemistry of spreadwing posture in birds. 3. Immunohistochemistry of flight
muscles and the “shoulder lock” in albatrosses. Journal of Morphology, 263: 12-29.
Moon, B.R. and Gans, C. (1998). Kinematics muscular activity and propulsion in gopher snake. Journal of Experimental Biology, 19: 2669-2684.
Mukund, K. and Subramaniam, S. (2020). Skeletal muscle: A review of molecular structure and function, in health and disease. Wiley Interdisciplinary Reviews in Systems Biology and Medicine, 12: e1462.
Periasamy, M., Herrera, J.L. and Reis, F. (2017). Skeletal muscle thermogenesis and its role in whole body energy metabolism. Diabetes and Metabolism Journal, 41: 327-336.
Peters S.E. (1989). Structure and function in vertebrate skeletal muscle. American Zoologist, 29: 221-234.
Purslow, P.P. (1989). Strain-induced reorientation of an intramuscular connective tissue network: implications for passive muscle elasticity. Journal of Biomechanics, 22: 21-31.
Purslow, P.P. (1999). The intramuscular connective tissue matrix and cell/matrix interactions in relation to meat toughness. In proceedings of 45th international congress of meat science and technology, 1-6 August 1999, Vol. 1, Yokohama, pp 210-219.
Purslow, P.P. (2020). The structure and role of intramuscular connective tissue in muscle function. Frontiers in
Physiology, 11(495): 1-15.
Rosser, B.W.C., Waldbillig, D.M., Wick, M. and Bandman, E. (1994). Muscle fiber types in the pectoralis of the white pelican, a soaring bird. Acta Zoology,75: 329-336.
Schmidt, R.E., Reavill, D.R. and David N. Phalen, D.N. (2015). Pathology of pet and aviary birds. Second Edition. JohnWiley & Sons, Inc, pp 199-220.
Scott, W., Stevens, J. and Binder-Macleod, S.A. (2001). Human skeletal muscle fiber type classifications. Physical Therapy, 81(11): 1810-1816.
Tani, S., Chung, U., Ohba, S. and Hojo, H. (2020). Understanding paraxial mesoderm development and sclerotome specification for skeletal
repair. Experimental and Molecular Medicine, 52: 1166-1177.
Williams T.M., Dobson, G.P., Mathieu-Costello, O., Morsbach, D., Worley M.B. and Phillips, J.A. (1997). Skeletal muscle histology and biochemistry of an elite sprinter, the African cheetah. Journal of Comparative Physiology B, 167: 527-535.
Wu, M.P., Chang, N.C., Chung, C.L., Chiu, W.C., Hsu, C.C., Chen, H.M., Sheu, J.R.,Jayakumar, T., Chou, D.S. and Fong, T.H. (2018). Analysis of titin in red and white muscles: crucial role on muscle contractions using a fish model.BioMed Research International, 2018: 1-11.