Sperm concentration, hyaluronic acid-binding capacity, aneuploidy and persistent histones in testicular cancer

Antibodies specifically reacting with the link proteins, the hyaluronic acid-binding region and chondroitin sulphate-peptides were used to design specific radioimmunoassay procedures. The sensitivity of the method used for the link protein was about 20 ng/ml, and the other two components could be determined at concentrations of about 2 ng/ml. The radioimmunoassay procedures were tested by using proteoglycan subfractions or fragments thereof. The procedures used to quantify link protein and hyaluronic acid-binding region showed no cross-interference. Fragments of trypsin-digested proteoglycan monomers still reacted in the radioimmunoassay for hyaluronic acid-binding region. Subfractions of proteoglycan monomers separated according to size had a gradually higher relative content of the hyaluronic acid-binding region compared with both chondroitin sulphate-peptides and uronic acid, when the molecules were smaller. The proteoglycans therefore may contain a variably large chondroitin sulphate-rich region, which has a constant substitution with polysaccharide side chains.

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Impaired Testicular Function in Patients With Carcinoma-In-Situ of the Testis

Journal of Clinical Oncology ◽

10.1200/jco.1999.17.1.173 ◽

1999 ◽

Vol 17 (1) ◽

pp. 173-173 ◽

Cited By ~ 71

Author(s):

Peter Meidahl Petersen ◽

Aleksander Giwercman ◽

Steen W. Hansen ◽

Jørgen G. Berthelsen ◽

Gedske Daugaard ◽

...

Keyword(s):

Testicular Cancer ◽

Germ Cell ◽

Leydig Cell ◽

Carcinoma In Situ ◽

Cell Function ◽

Semen Quality ◽

Sperm Concentration ◽

Testicular Dysfunction ◽

Leydig Cell Function

PURPOSE: To elucidate the biologic association between germ cell neoplasia and testicular dysfunction, through investigation of Leydig cell function and semen quality in men with carcinoma-in-situ (CIS) of the testis. PATIENTS AND METHODS: We examined two groups of men, unilaterally orchidectomized for testicular cancer. Biopsy of the contralateral testis had showed CIS in a group of 24 patients and no evidence of CIS in the other group of 30 patients. Semen quality and serum levels of testosterone, luteinizing hormone (LH), and follicle-stimulating hormone (FSH) were compared in these two groups of men after orchidectomy but before further treatment for testicular cancer. RESULTS: Significantly higher LH levels (median, 8.1 IU/L v 4.8 IU/L; P < .001) and generally lower testosterone levels (median, 12.5 nmol/L v 15.5 nmol/L; P = .13) were found in the CIS group. The proportion of patients with Leydig cell dysfunction was higher in the group of patients with CIS (11 of 24) than in the group of patients without (two of 30) (P = .01). Sperm concentration and total sperm count were significantly lower (P < .001) in patients with CIS (median, 0.03 × 106/mL and 0.10 × 106, respectively) than in patients without (median, 9.1 × 106/mL and 32 × 106, respectively), whereas the levels of FSH were significantly higher (P < .001) in the former group of men (median, 19.6 IU/L v 9.0 IU/L). CONCLUSION: Not only spermatogenesis but also Leydig cell function is impaired in testes with CIS. This impairment could be due to common factors in the pathogenesis of germ cell neoplasm and testicular dysfunction. Alternatively, CIS cells may have a negative impact on Leydig cell function.

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The properties of proteoglycan prepared from human articular cartilage by using associative caesium chloride gradients of high and low starting densities

Biochemical Journal ◽

10.1042/bj2320111 ◽

1985 ◽

Vol 232 (1) ◽

pp. 111-117 ◽

Cited By ~ 25

Author(s):

M T Bayliss ◽

P J Roughley

Keyword(s):

Hyaluronic Acid ◽

Articular Cartilage ◽

Proteinase Inhibitors ◽

Density Gradient Centrifugation ◽

Gradient Centrifugation ◽

Human Articular Cartilage ◽

Adult Human ◽

Cscl Density Gradient ◽

Proteoglycan Aggregates ◽

Hyaluronic Acid Binding

Proteoglycan was extracted from adult human articular cartilage from both the knee and the hip, and A1 preparations were prepared by CsCl-density-gradient centrifugation at starting densities of 1.69 and 1.5 g/ml. Irrespective of whether the cartilage was diced to 1 mm cubes or sectioned to 20 micron slices there was always a lower proportion of both protein and proteoglycan aggregate in the A1 preparation prepared at 1.69 g/ml. Furthermore, the addition of exogenous hyaluronic acid to the extracts before centrifugation did not improve the yield of aggregate at 1.69 g/ml. These results were not affected by the presence of proteinase inhibitors in the extraction medium. It appears that adult human articular cartilage contains a high proportion of low-density proteoglycan subunits and hyaluronic acid-binding proteins that make most of the re-formed proteoglycan aggregates of a lower density than is usually encountered with younger human and mammalian hyaline cartilages.

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