Effect of peptides of bovine myelin basic protein on dermal fibroblasts
β Scribed by Dr. T. M. Chiang; J. N. Whitaker; J. M. Seyer; A. H. Kang
- Publisher
- John Wiley and Sons
- Year
- 1980
- Tongue
- English
- Weight
- 413 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0360-4012
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β¦ Synopsis
Abstract
Bovine basic protein (BP) was digested with purified bovine brain cathepsin D to produce well defined BP derived peptides 1β42, 43β88, 43β169, and 89β169. BP and these BP peptides were tested for their effects on cultured human dermal fibroblasts using a concentration range of 0.01β1,000 ng/ml. No effect was found on cellular proliferation, and neither total protein nor collagen synthesis was altered in the presence of these substances. Although preparations of brain which contain a fibroblastβgrowth factor also contain BP peptides, these results indicate that the purified BP peptides studied have no detectable biological effect on the growth of human dermal fibroblasts.
π SIMILAR VOLUMES
The interaction of myelin basic protein with cholesterol and the conformational changes occurring in the protein upon interaction with the lipid were investigated. The myelin basic protein (MBP) plays an important role in stabilizing the multilamellar structure of the myelin membrane. MBP interacts
## Synopsis Myelin basic protein isolated from bovine white matter is known to consist of a mixture of three or more "charge isomers," which can be separated by cation-exchange chromatography. We are using 360-MHz 'H-nmr spectroscopy to establish the chemical and structural differences among them.
## Abstract In order to determine the peptide bond specificity of calpain, human myelin basic protein (HMBP) was treated with purified calpain of bovine brain. Upon incubation, HMBP component I (HMBPβ1) was degraded into several peptides as demonstrated by sodium dodecy1 sulfateβpolyacrylamide gel