Lysosomal enzyme activities: new potential markers for Sjögren's syndrome.

Objective: To evaluate the changes in lysosomal enzyme activities in leukocytes of patients with Sjögren's syndrome.

Methods: Leukocytes were obtained from 38 patients with Sjögren's syndrome and 36 healthy subjects. The activities of the following glycosidases were measured: alpha-glucosidase (AGU), beta-galactosidase (BGA), alpha-mannosidase (AMAN), beta-glucuronidase (GCU), beta-hexosaminidase (HEX), and the following proteases: cathepsin B (CATH B), dipeptidyl peptidase I (DPP I), cathepsin H (CATH H), dipeptidyl peptidase II (DPP II), tripeptidyl peptidase I (TPP I), and cathepsin D (CATH D) activity.

[Second primary malignant tumors in patients with ocular melanoma].

Multiple primary malignant tumors have been documented with increased frequency over the last two decades. Continuously increasing success of modern oncotherapy has led to long-term remissions in many cases, but this success rate poses a growing risk for the development of second primary malignancies. The incidence of those involving an intraocular tumor is relatively rare.

[Connection between uveal melanoma and dysplastic naevus syndrome].

The dysplastic naevus syndrome increases the risk of cutaneous (RR: 4.36; CI: 1.84-10.

Ocular pigmented findings in patients with dysplastic naevus syndrome.

There is a growing body of evidence supporting the theory that cutaneous dysplastic naevus syndrome patients are at increased risk of developing not only skin but also uveal melanoma. The relationship between dysplastic naevus syndrome and ocular naevi needs to be clarified. In this study we investigated the ocular pigmented findings in patients with dysplastic naevus syndrome and compared the results with a control group (subjects without atypical moles) in order to investigate the frequency of ocular naevi among dysplastic naevi-bearing patients.

Lysosomal peptidases and glycosidases in rheumatoid arthritis.

Lysosomal serine and cysteine proteases are reported to play a role in collagen degradation. In this study, the activities of the lysosomal cysteine proteases cathepsin B and H, dipeptidyl peptidase I, and the serine protease tripeptidyl peptidase I and dipeptidyl peptidase II, all ascribed a role in collagen digestion, were compared with those of the aspartate protease cathepsin D, and lysosomal glycosidases in leukocytes from rheumatoid arthritis patients at different stages of the disease. In all patients the activities of cysteine protease cathepsin B, dipeptidyl peptidase I, aspartate protease cathepsin D, and two glycosidases were elevated, but the activities of the serine proteases tripeptidyl peptidase I, dipeptidyl peptidase II, and the cysteine protease cathepsin H was unchanged.