scholarly journals Studies on the assembly of the rat lens capsule. Biosynthesis of a cross-linked collagenous component of high molecular weight

1980 ◽  
Vol 190 (2) ◽  
pp. 229-237 ◽  
Author(s):  
J G Heathcote ◽  
A J Bailey ◽  
M E Grant

1. Intact rat lenses in tissue culture synthesize hydroxy[3H]proline-containing polypeptides of apparent mol.wt. approx. 180000, which become assembled into aggregates of higher molecular weight with time. 2. Both the 180000-mol.wt. species and the aggregates are components of the deoxycholate-insoluble base-membrane matrix. 3. Formation of the high-molecular-weight aggregate is accompanied by the biosynthesis of the reducible hydroxylysine-derived cross-link hydroxylysino-5-oxo-norleucine. 4. Hydroxylysino-5-oxonorleucine and dehydrohydroxylysinonorleucine are the major reducible cross-links present in intact foetal and 1-month-old calf lens capsules.


1975 ◽  
Vol 149 (1) ◽  
pp. 289-291 ◽  
Author(s):  
G M Blackburn ◽  
P E Taussig

Anthracene becomes covalently bound to high-molecular-weight DNA in mammalian tissue culture as a result of irradiation at 365 nm after the incubation of cells with the hydrocarbon. At high radiation doses, the extent of binding exceeds one hydrocarbon molecule per 103 bases, and is lethal. At low radiation doses, much decreased binding is observed, but a majority of cells remain viable and can be recultured.





1973 ◽  
Vol 21 (3) ◽  
pp. 199-208 ◽  
Author(s):  
RUSSELL ROSS

A number of important questions remain to be answered concerning our understanding of elastic tissues. The size and molecular weight of the elastin precursor remains to be clearly established. The number of proteins involved in the microfibrillar component of the elastic fiber are as yet undetermined, although it would appear that they are glycoproteins that may represent a species of reasonably high molecular weight. Clearly the elastic fiber contains two morphologic components. During morphogenesis, the elastic fiber begins to appear in the form of aggregates of microfibrils that take the shape and direction of the presumptive elastic fiber. With increasing maturity elastin begins to form within the interstices of each bundle of microfibrils. By the time the elastic fiber is fully formed it consists largely of the amorphous component, elastin, surrounded by an envelope of microfibrils with microfibrils embedded within its interstices. It has been suggested that the microfibrils form and take their shape extracellularly under the influence of the cells that have secreted their precursors. After the aggregates of microfibrils have taken their shape Ross and Bornstein (22) have suggested that the elastin may interact ionically with the surface of the microfibrils, since each of these two components has an opposite net charge, and may be held in position while desmosine cross-links are established through the action of the enzyme, lysyl oxidase. Thus the microfibrils would serve as a scaffolding to determine morphogenetically the shape and direction to be later taken by the mature elastic fiber. The reason for the elastic properties of the elastin is still yet poorly understood, and the means by which the cells synthesize and secrete both of these components remain to be investigated.





1978 ◽  
Vol 47 (6) ◽  
pp. 1390-1393 ◽  
Author(s):  
XAVIER Y. BERTAGNA ◽  
WENDELL E. NICHOLSON ◽  
OLIVE S. PETTENGILL ◽  
GEORGE D. SORENSON ◽  
CHARLES D. MOUNT ◽  
...  


1993 ◽  
Vol 4 (3) ◽  
pp. 293-299 ◽  
Author(s):  
S.D. Bradway ◽  
M.J. Levine

Previously, we reported that a membrane-bound epithelial enzyme, transglutaminase (TGase), catalyzes the covalent cross-linking of acidic proline-rich proteins (APRPs) to surface proteins of buccal epithelial cells (BECs). The purpose of this study was twofold: (1) to provide evidence that TGase stabilizes C. albicans adhesion by covalently cross-linking C. albicans and BEC surface proteins and (2) to implicate PRPs in the modulation of this adhesive mechanism. The reactivity of candidal cell wall proteins with TGase was assessed in two separate experiments. Initially, following incubation with native BECs, the cross-linking of iodinated candidal cell wall proteins into high-molecular-weight complexes, as shown by SDS-PAGE/ autoradiography, was inhibited by the TGase inhibitor iodoacetamide. Additionally, [14C]putrescine in the presence of purified TGase, but not [14C]putrescine alone, was shown by SDS-PAGE/fluorography to be cross-linked into surface proteins of both morphogenetic forms (blastospore > hyphal forms) of C. albicans. In adherence assays, a component of both blastospore and hyphal form Candida/BEC adherence was shown to be resistant to detachment by heating adherent cells in 1% SDS at 100°C. However, pretreatment of BECs with iodoacetamide decreased SDS resistant adherence of both forms of C. albicans by =75%. When incubated with [125I]APRPs and purified TGase, both morphogenetic forms of C. albicans bound dramatically more APRP than controls without TGase. [125I]APRP binding in experimental, but not control, samples was resistant to repeated extraction (48 h) with 4% SDS/10% β-mercaptoethanol at 65°C, suggesting that [125I]APRPs were cross-linked to the Candida surface. SDS-PAGE/fluorography was used to verify that APRPs, in Lyticase digests of Candida cell walls, were cross-linked into a high-molecular-weight complex. These experiments suggest that epithelial TGase may stabilize Candida adherence by cross-linking Candida and BEC surface proteins. Additionally, because TGase cross-links APRPs to candidal and epithelial surface proteins, APRPs may interfere with TGase catalyzed mechanisms of adhesion. Supported by USPHS grants DE00185, DE07585, and OSU Seed grant.



2015 ◽  
Vol 45 ◽  
pp. 174-178 ◽  
Author(s):  
Steven D. Reinitz ◽  
Evan M. Carlson ◽  
Rayna A.C. Levine ◽  
Katherine J. Franklin ◽  
Douglas W. Van Citters


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