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At least 379 records · Page 21Linked to original sources
PubMed1976

Experimental allergic aspermatogenic orchitis. IV. Chemical properties of sperm glycoproteins isolated from guinea pig testes.

Of four glycoproteins isolated from guinea pig testes, two were aspermatogenic (types I and IV) and two (types II and III) were inactive. The glycoproteins were rich in carbohydrate, varying from 41.5% to 49.5% carbohydrate by weight. Each glycoprotein had a unique amino acid composition, but in general low levels of tyrosine, tryptophan, and basic amino acids were found along with relatively high contents of serine, threonine, glutamic acid, and proline. Types I and IV glycoproteins were remarkably stable; their aspermatogenic activity was not affected by urea, trypsin, or heating at 100 degrees C in water or in 1 M HCl for 15 min. Carbohydrate analysis revealed little difference in the monosaccharide compositions of types I and IV glycoproteins, except that only the type I contained sialic acid. In contrast, types II and III glycoproteins lacked sialicacid and fucose and contained much less mannose. Both N-acetylglucosamine and N-acetylgalactosamine were present in all four glycoproteins, and they dominated in the types II and III. Fucose and at least 20-25% of the galactose appeared to occupy terminal positions in type IV glycoprotein as shown by their release after 15 min hydrolysis in 1 M HCl. All of the glycoproteins contained a relatively high percentage of galactose by weight, from 12.6 to 19.3%. The molecular weights of the glycoproteins were estimated by sodium dodecyl sulfate gel electrophoresis to be 47000, 105000 and 18000 respectively for the types I, II, and IV; type III glycoprotein showed two major bands, with molecular weights of 41500 and 22800. All the above molecular weight values are probably overestimated because of high carbohydrate content. The molecular weight of type IV glycoprotein was found to be 13000 by ultracentrifugation; a corrected value of 29000 was calculated for type I glycoprotein.

Amino Acids↗
PubMed1976

Experimental allergic aspermatogenic orchitis. II. Some chemical properties of the AP1 protein of the sperm acrosome.

The AP1 protein, a unique aspermatogenic protein localized in the sperm acrosome, exists as a single polypeptide chain of 136 amino acids, as shown by a single band on gel electrophoresis in sodium dodecyl sulfate and the recovery of the expected 21 to 22 tryptic peptides on peptide mapping. The AP1 protein appears to exist in a compact, highly stable conformation, as shown by its resistance to trypsin hydrolysis. Its aspermatogenic acitivity is not affected by trypsin treatment, by heating at 99 degrees C for 1 h, by 8 M urea, or by acid conditions. After reduction and alkylation, however, the molecule appears to open up, since it becomes hydrolyzable by trypsin and migrates more slowly on gel electrophoresis at pH 2.7 and 8.6. After alkylation, the AP1 protein still migrates as a single band at pH 2.7. The AP1 protein shows microheterogeneity near its isolectric point at pH 8.6; each of five bands shows the same amino acid analysis. Aggregation was not observed following treatment with dimethylsuberimidate. The molecular weight of 15 000, obtained from gel electrophoresis consists of 136 amino acids with a relatively high content of proline, half cystine, glycine, histidine and tryptophan. No galactose, mannose, fucose, glucose, or hexosamines were found; the AP1 protein is thus not a glycoprotein.

Acrosome↗
PubMed1988

Tuberculous epididymo-orchitis.

In the clinical course of epididymitis in a forty-four-year-old male patient, enlargement of ipsilateral testis developed which was difficult to distinguish clinically from testicular tumor. High inguinal orchiectomy was performed. Microscopic sections revealed many granulomas with caseous necrosis and giant cells. Tuberculous bacilli also were demonstrated in the histologic examination.

Adult↗
PubMed1990

Mumps orchitis.

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Adolescent↗
PubMed1986

Macrophage activation during experimental allergic orchitis in rainbow trout (Salmo gairdneri).

Macrophages isolated from fish undergoing an experimentally induced autoimmune response against the testis were found to have been activated using several morphological and functional criteria. They exhibited increases in cell spreading, phagocytosis, reduction of nitroblue tetrazolium and acid phosphatase activity. In addition they possessed larger and more numerous cytoplasmic organelles and peripheral processes compared with control cells. Culture of the autoimmunologically elicited cells for 1 or 2 days resulted in their return to a non-activated state.

Acid Phosphatase↗
PubMed2001

[Xanthogranulomatous orchitis. Report of 7 cases].

The xanthogranulomatosis orchiepididymititis is a benign and a rare disease. Its etiology is unknown. It creates diagnosis, therapeutic and etiological problems. The diagnosis is hardly made because of the variability of the clinical findings. The confusion is mainly made with a malignant tumor, and sometimes with a simple orchiepididymitis. Orchidectomy is usually performed. We report seven cases of orchiepididymitis characterized by their antibiotherapeutic resistance, the destruction of the testis which needed a surgical removal. The diagnosis is established after the histological study of the testis. The etiology is not yet known. The authors study the clinical evolution and therapeutic characteristics of our serial comparing with the literature data.

Adult↗