Isolation of lipocalin-type protein from rainbow trout seminal plasma and its localisation in the reproductive system
Joanna Nynca A C , Mariola A. Dietrich A , Barbara Bilińska B , Małgorzata Kotula-Balak B , Tomasz Kiełbasa A , Halina Karol A and Andrzej Ciereszko A
+ Author Affiliations
- Author Affiliations
A Department of Gamete and Embryo Biology, Semen Biology Group, Institute of Animal Reproduction and Food Research, Tuwima 10, 10‐747 Olsztyn, Poland.
B Department of Endocrinology, Institute of Zoology, Jagiellonian University, 30‐060 Krakow, Poland.
C Corresponding author. Email: j.nynca@pan.olsztyn.pl
Reproduction, Fertility and Development 23(2) 381-389 https://doi.org/10.1071/RD10118
Submitted: 26 May 2010 Accepted: 1 September 2010 Published: 4 January 2011
Abstract
The lipocalin protein family is a large and diverse group of small extracellular proteins characterised by their ability to bind hydrophobic molecules. In the present study, we describe the isolation procedure for rainbow trout seminal plasma protein, characterised by a moderate migration rate during polyacrylamide gel electrophoresis, providing information regarding its basic features and immunohistochemical localisation. This protein was identified as a lipocalin-type protein (LTP). The molecular mass of LTP was found to be 18 848 Da and it was found to lack any carbohydrate components. Only a few Salmoniformes contain LTP in their seminal plasma. The abundance of LTP in the Sertoli and Leydig cells of the testes of the rainbow trout, as well as in secretory cells of the efferent duct, suggests that this protein is specific for rainbow trout milt, where it acts as a lipophilic carrier protein. Moreover, the specific localisation of LTP in the flagella of the spermatozoa suggests a role for LTP in sperm motility. Further experiments are necessary to identify the endogenous ligands for LTP in rainbow trout seminal plasma and to characterise the binding properties of this protein.
Additional keywords: fish, immunohistochemistry, LTP, milt, polyclonal antibodies, purification.
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