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AARNE I. KOSKIMIES and MARTTI KORMANO

Department of Anatomy, University of Helsinki, Finland

(Received 21st October 1974)

The fluid transporting spermatozoa out of the testis through the epididymis is known to undergo many changes. About 50% of the fluid secreted by the seminiferous tubules is reabsorbed by the first part of the epididymal duct system (Crabo & Gustafsson, 1964; Levine & Marsh, 1971). Between the caput epididymidis and the ductus deferens, a further 50% of the remaining fluid is reabsorbed.

Seminiferous tubule fluid and rete testis fluid contain several protein fractions not seen in the serum, as has been shown by polyacrylamide gel electrophoresis (Kormano, Koskimies & Hunter, 1971; Koskimies & Kormano, 1973). The fate and significance of most of these proteins is unknown. Recently, it has been shown electrophoretically that bovine epididymal plasma from the cauda region contains at least three proteins not detected in the rete testis fluid or serum (Amann, Killian & Benton,

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AARNE I. KOSKIMIES and MARTTI KORMANO

Summary.

Proteins in fluids from the seminiferous tubules and rete testis of rats were studied with a high resolution electrophoretic technique, utilizing a step gradient, polyacrylamide gel system. Both fluids contained a number of specific bands, i.e. proteins not seen in serum or in intratesticular lymph. The rete testis fluid contained more serum proteins than the seminiferous tubule fluid. The albumin—globulin ratio was also greater in the former fluid. Two-dimensional separations showed that the bulk of specific proteins moved as prealbumins. Strong esterase and acid phosphatase activities were located in the region of the specific proteins with the intermediate mobility in acrylamide gel. The origin of these proteins and their significance is discussed in relation to the functional differences between the seminiferous tubules and the rete testis.

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AARNE I. KOSKIMIES, MARTTI KORMANO and AITO LAHTI

Seminiferous tubule fluid of the testis is unique in many respects, due to the existence of a barrier mechanism which prevents the entry of various endogenous and administered substances (for references, see Setchell, 1970). Recent studies on ram rete testis fluid obtained by catheter implantation technique (Voglmayr, Waites & Setchell, 1966), suggest that all the individual serum proteins are present in the rete testis fluid but in much lower concentrations. The existence of a specific protein was reported by Johnson & Setchell (1968). Assuming that the rete testis fluid might represent the fluid secreted by the seminiferous tubules, Johnson & Setchell (1968) came to the conclusion that a very little immunoglobulin does enter into the seminiferous tubule fluid, immunoglobulin being observed in the immunoelectrophoretic study of the rete testis fluid. However, in

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AARNE I. KOSKIMIES, MARTTI KORMANO and OLOF ALFTHAN

Summary.

Seminiferous tubule fluid was collected by micropuncture from ten human testes immediately after orchidectomy and subjected to high resolution step gradient acrylamide gel electrophoresis. The protein patterns of the fluid were compared with those of serum and intratesticular lymph. The seminiferous tubule fluid always contained a number of proteins not seen in serum or in testicular lymph and a few proteins which were electrophoretically identical with those in serum. The bulk of these relatively weak serum bands consisted of albumin. Disturbance of spermatogenesis did not influence either the appearance of specific proteins or the degree of serum contamination.

The present results are interpreted to mean that in man, as in animals, there is an effective blood—testis barrier. The specific proteins of the seminiferous tubules may be elaborated by Sertoli cells.