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Exposure of an arginine-rich protein at surface of cells in S, G2, and M phases of the cell cycle

✍ Scribed by Sylvia M. Stein; John M. Berestecky

Book ID
102883538
Publisher
John Wiley and Sons
Year
1975
Tongue
English
Weight
565 KB
Volume
85
Category
Article
ISSN
0021-9541

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✦ Synopsis

Abstract

Phenylglyoxal (PG) is shown to be a cell surface probe specific for arginine moieties in protein: (1) It does not enter the cell as evidenced by lack of PG in the cytoplasm. (2) It does not cause excessive cell leakage as measured by release of ^51^Cr. (3) It reacts with positively‐charged groups in proteins at the cell surface but not with those of phospholipids at the surface; since pronase removes PG from the surface, but phospholipase C does not. (4) Under the conditions used in these experiments, it reacts virtually exclusively with arginine moieties in protein (Freedman et al., '68; Takahashi, '68; Werber and Sokolovsky, '72).

Synchronized cells were exposed to radioactive PG to assess quantity of arginine moieties in protein at the surface. There is a sharp decrease in arginine at the cell surface at entry into G~1~ phase from M and a 24‐fold increase upon entry into S phase. There is a slight drop in exposed arginine in late S phase followed by an increase to 26 times the G~1~ level immediately prior to mitosis. Lactoperoxidase‐catalyzed iodination of tyrosine moieties in protein at the surface of synchronized cells shows a very gradual increase in protein as the cells move through the cycle and increase in size. Since the increase in arginine moieties in protein at the surface does hot reflect a similar increase in total protein at the surface, an arginine‐rich protein appears to be exposed at the cell surface during the division‐related phases of the cell cycle.

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