1984
DOI: 10.1016/0014-5793(84)81147-3
|View full text |Cite
|
Sign up to set email alerts
|

Biosynthesis of intestinal microvillar proteins

Abstract: Using alkaline extraction to separate cytoskeletal and membrane proteins of intestinal microvilli, the kinetics of assembly of these two microvillar protein compartments was studied by pulse-chase labelling of pig small intestinal mucosal explants, kept in organ culture. Following a 10 min pulse of [35S]methionine, the membrane proteins did not appear in the microvillar fraction until after 40-60 min of chase. In contrast, the cytoskeletal components, of which the llO-kDa protein and villin were immunologicall… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
4
0

Year Published

1985
1985
2007
2007

Publication Types

Select...
4
2
1

Relationship

1
6

Authors

Journals

citations
Cited by 21 publications
(4 citation statements)
references
References 27 publications
0
4
0
Order By: Relevance
“…large amounts of keratin mRNAs may be required to preserve cellular architecture and terminal web organization in the presence of a rapid turnover of brush border cytoskeletal proteins [57,58]. Such processes may extend to keratin-related polypeptides and be responsible, at least in part, for the increased complexity of the two-dimensional immunoblots.…”
Section: Discussionmentioning
confidence: 99%
“…large amounts of keratin mRNAs may be required to preserve cellular architecture and terminal web organization in the presence of a rapid turnover of brush border cytoskeletal proteins [57,58]. Such processes may extend to keratin-related polypeptides and be responsible, at least in part, for the increased complexity of the two-dimensional immunoblots.…”
Section: Discussionmentioning
confidence: 99%
“…5), but differed markedly from the faint labelling seen in the lane showing non-specifically aggregated material in the gel. Amongst the major bands immunoprecipitated were the 166000-M, and 140000-M, polypeptides of aminopeptidase N. In addition, many other polypeptides were precipitated; one, of about M , 240000 represents the transient and mature forms of sucrase-isomaltase and iiialLase-glucoamylase, and some, in particular those of M , 105000 (1 10-kDa protein), M , 95000 (villin) and Mr 40000 (actin), are likely to correspond to microvillar cytoskeletal components which are known to become labelled within 10 min [17]. Other bands probably correspond to co-precipitated proteins of various intracellular membranes.…”
Section: Immunoelectrophoretic Isolation Of'nzernbrancs Harbouring MImentioning
confidence: 99%
“…Such an assignment has implications not only for its role in brush border structure and function but also for its synthesis, transport, and compartmentalization within the cell. In fact, Cowell and Danielsen [26,27] have recently provided biosynthetic data to suggest that llOK, like villin and actin, probably is not synthesized on the rough ER, as is typical for integral membrane proteins, but rather is synthesized on free ribosomes. This would suggest that the llOK either is a peripheral membrane protein or is inserted into the membrane posttranslationally, as has been demonstrated for the microsomal membrane proteins cytochrome b5 and NADH:cytochrome b5 oxidoreductase [see 26,27 for discussion].…”
Section: Discussionmentioning
confidence: 99%