Paper category: Original research paper
Corresponding author: Agnieszka Kąkol (firstname.lastname@example.org)
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Citation: Kąkol, A. & Szaniawska, A. (2019). Crangon crangon: can hydroxyproline be an indicator of changes in the species?. Oceanological and Hydrobiological Studies, 48(2), pp. 116-124. Retrieved 3 Oct. 2019, from doi:10.1515/ohs-2019-0012
The hydroxyproline content in Crangon crangon tissues from the Gulf of Gdańsk (southern Baltic) was determined in males, non-ovigerous females and ovigerous females, depending on the individual body length, the study area (two profiles: Gdynia and Sopot) and the depth of occurrence. Individuals were collected and analyzed from April to August 2008. The research on the migratory species C. crangon indicates that the area and depth of its occurrence do not significantly affect the level of hydroxyproline in the tissues of this animal (p > 0.05). However, certain trends have been observed. Hydroxyproline participates in various life processes of C. crangon and its level in the tissues is significantly correlated with the sex of animals (p < 0.05). In males, hydroxyproline plays a major role in the body growth. Moreover, water temperature significantly affects the hydroxyproline content in males of different body sizes. Ovigerous females use hydroxyproline in the reproductive process. In non-ovigerous females, hydroxyproline participates both in the growth of organisms and in the reproductive period. Hydroxyproline can be an indicator of the collagen level, as well as an important factor in physiological processes.
Akel, P.J. (1981). Characterization of the collagen protein in smooth pink shrimp (Pandalus jordani). Master Thesis (pp. 68), Oregon State University, United States.
Brauer, J.M.E., Leyva, J.A.S., Alvarado, L.B. & Sández, O.R. (2003) Effect of dietary protein on muscle collagen, collagenase and shear force of farmed white shrimp (Litopenaeus vannamei). Eur. Food Res. Tech. 217: 277–280. DOI: 10.1007/s00217-003-0739-7.
Czarnowski, W. & Krechniak, J. (1989). Hydroxyproline and urinary fluoride in rats repeatedly exposed to inhaled phosphorites. Fluoride 22(1): 24–28.
Féral, J.-P. (1988). Wound healing after arm amputation in Sepia officinalis (Cephalopoda: Sepioidea). J. Invert. Pathol. 52: 380–388. DOI: 10.1016/0022-2011(88)90049-3.
Furukawa, Y., Honma, Y. & Kimura, S. (1973). Age-dependent changes on insoluble collagen of the skin of rats. Tohoku J. Agri. Res. 23(4): 216–223.
Heu, M.S., Kim, J.S. & Shahidi, F. (2003). Components and nutritional quality of shrimp processing by-products. Food Chem. 82: 235–-242. DOI: 10.1016/S0308‑8146(02)00519‑8.
Holthuis, L.B. (1980) FAO Species catalogue. vol. 1. Shrimps and prawns of the world. An annotated catalogue of species of interest to fisheries, The Food and Agriculture Organization of the United Nations. Rome. pp. 271.
Hulmes, D.J.S. (2008). Collagen diversity, synthesis and assembly. In P. Fratzl (Ed.), Collagen. Structure and Mechanics (pp. 15–41), New York: Springer.
Ignat’eva, N.Yu., Danilov, N.A., Averkiev, A.V., Obrezkova, M.V., Lunin, V.V. et al. (2007). Determination of hydroxyproline in tissues and the evaluation of the collagen content of the tissues. J. Anal. Chem. 62(1): 51–57.
Jeffery, S. & Revill, A. (2002). The vertical distribution of southern North Sea Crangon crangon (brown shrimp) in relation to towed fishing gears as influenced by water temperature. Fish. Res. 55: 319–323. DOI: 10.1016/S0165-7836(01)00297-1.
Kavitha, O. & Thampan, R.V. (2008). Factors influencing collagen biosynthesis. J. Cell. Biochem. 104: 1150–1160. DOI: 10.1002/jcb.21728.
Kurita, K. (2006). Chitin and chitosan: Functional biopolymers from marine crustaceans. Mar. Biotechnol. 8: 203–226. DOI: 10.1007/s10126-005-0097-5.
Lloyd, A.J. & Yonge, C.M. (1947). The biology of Crangon vulgaris (Linneaus, 1958) in the Bristol Channel and Severn estuary. J. Mar. Biol. Ass. U.K. 26: 626–661.
Łapińska, E. & Szaniawska, A. (2006). Environmental preferences of Crangon crangon (Linnaeus, 1758), Palaemon adspersus Rathke, 1837, and Palaemon elegans Rathke, 1837 in the littoral zone of the Gulf of Gdańsk. Crustaceana. 79(6): 649–662. DOI: 10.1163/156854006778026799.
Mizuta, S., Miyagi, T. & Yoshinaka, R. (1998). Characterization of a major alpha component of collagen from muscle of Antarctic krill Euphausa superba. Comp. Biochem. Physiol. 120B: 597–604.
Morales, J., Montero, P. & Moral, A. (2000). Isolation and partial characterization of two types of muscle collagen in some cephalopods. J. Agri. Food Chem. 48: 2142–2148. DOI: 10.1021/jf990711k.
Muyonga, J.H., Cole, C.G.B. & Duodu, K.G. (2004). Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chem. 85: 81–89. DOI: 10.1016/j.foodchem.2003.06.006.
Neuman, R.E. & Logan, M.A. (1949). The determination of hydroxyproline. J. Biol. Chem. 299–306.
Oh, C.-W. & Hartnoll, R.G. (2004). Reproductive biology of the common shrimp Crangon crangon (Decapoda: Crangonidae) in the central Irish Sea. Mar. Biol. 144: 303–316. DOI: 10.1007/s00227-003-1205-6.
Oh, C.W., Hartnoll, R.G. & Nash, R.D.M. (1999). Population dynamics of the common shrimp, Crangon crangon (L.) in Port Erin Bay, Isle of Man, Irish Sea. ICES J. Mar. Sci. 56: 718–733. DOI:10.1006/jmsc.1999.0501.
Revill, A.S. & Holst, R. (2004). Reducing discards of North Sea brown shrimp
(C. crangon) by trawl modification. Fish. Res. 68: 113–122. DOI: 10.1016/j.fishres.2004.02.001.
Sachindra, N.M., Bhaskar, N. & Maheendrakar, N.S. (2005). Carotenoids in different body components of indian shrimps. J. Sci. Food Agri. 85: 167–172.
Sato, M., Yoshinaka, R. & Ikeda, S. (1978). Dietary ascorbic acid requirement of rainbow trout for growth and collagen formation. Nippon Suisan Gakkaishi 44: 1029–1035. DOI: 10.2331/suisan.58.671.
Siddiqi, N.J., Sharma, B. & Alhomida, A.S. (2001). A study on distribution of different hydroxyproline fractions in the bovine ocular tissues. Mol. Cell. Biochem. 217: 67–71. DOI: 10.1023/A:1007236301956.
Sivakumar, P. & Chandrakasan, G. (1999). Marine invertebrate collagens: The prevalence of type V and XI like collagen in some marine crustacean and molluscan tissues. Proc. Indian Acad. Sci. (Chem. Sci.) 111(1): 87–104.
Sivakumar, P., Suguna L. & Chandrakasan, G. (1997). Purification and partial characterization of a type V like collagen from the muscle of marine prawn Penaeus indicus. J. Biosci. 22(2): 131–141. DOI: 10.1007/BF02704727.
Shuster, S., Black, M.M. & McVitie, E. (1975). The influence of age and sex on skin thickness, skin collagen and density. Brit. J. Dermatol. 93: 639–643. DOI: 10.1111/j.1365-2133.1975.tb05113.x.
Sriket, P., Benjakul, S., Visessanguan, W. & Kijroongrojana, K. (2007). Comparative studies on chemical composition and thermal properties of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) meats. Food Chem. 103: 1199–1207. DOI: 10.1016/j.foodchem.2006.10.039.
Stegemann, H. (1958). Microdetermination of hydroxyproline with chloramine-T and p-dimethylaminobenzaldehyde. Hoppe Seylers Z. Physiol. Chem. 311: 41–45.
Tiews, K. (1970). Synopsis of biological data on the common shrimp Crangon crangon (Linneaus, 1758). FAO Fish. Rep. 57(4): 1167–1224.
Touhata, K., Tanaka, M., Toyohara, H., Tanaka, H. & Sakagichi, M. (2000). Seasonal change in collagen content of red seabream muscle. Fish. Sci. 66: 553–557.
Toyohara, H., Ito, K., Touhata, K., Kinoshita, M., Kubota, S. et al (1997). Effect of maturation on the contents of free and bound forms of hydroxyproline in ayu muscle. Fish. Sci. 63(9): 843–844.
Vasanthakumar, G., Chandrakasan, G. & Krishnan, G. (1980). A comparative study of the composition of the collagens of the foot of two lamellibranch molluscs occurring in different habitats. J. Biosci. 2(4): 299–304.
Yoshinaka, R., Sato, K., Itoh, Y., Nakajima, S. & Sato, M. (1989) Content and partial characterization of collagen in crustacean muscle. Comp. Biochem. Physiol. 94B: 219–223. DOI: 10.1016/0305-0491(89)90037-0.
Żmudziński, L. & Ostrowski, J. (1990). Zoobenthos. In A. Majewski. (Ed.), Gdańsk Bay (pp. 402–430), Warszawa: Wyd. Geol. (In Polish).