NDLI: Charge reversal at the P3' position in protein C optimally enhances thrombin affinity and activation rate.

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Charge reversal at the P3' position in protein C optimally enhances thrombin affinity and activation rate.

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Charge reversal at the P3' position in protein C optimally enhances thrombin affinity and activation rate.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gerlitz, B. Grinnell, B. W. Richardson, M. A.
Description	Author Affiliation: Richardson MA ( Lilly Research Laboratories, Lilly Corporate Center, Indianapolis, Indiana 46285-0434.)
Abstract	We have examined the properties of several human protein C (HPC) derivatives with substitutions for acidic residues near the thrombin cleavage site, including changing the P3' Asp to Asn (D172N), Gly (D172G), Ala (D172A), or Lys (D172K). The rate of thrombin-catalyzed activation of D172N, D172G, and D172A was increased 4-9-fold compared to wild-type HPC, primarily due to a reduction in the inhibitory effect of calcium and a resulting increase in affinity for free alpha-thrombin. There was no significant increase in activation rate or affinity with these 3 derivatives in the absence of calcium, confirming that P3' Asp affects calcium dependency in the native protein C molecule. With charge reversal at P3' (D172K), there was a 30-fold increase in activation rate in the presence of calcium, but unlike the other derivatives, there was a substantial effect (5-fold) on the activation rate and affinity for free alpha-thrombin in the absence of calcium. Thus, protein C affinity for thrombin appears to be influenced by a combination of calcium-dependent and -independent effects of the acidic P3' residue.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein C Chemistry Thrombin Metabolism Amino Acid Sequence Binding Sites Calcium Pharmacology Electrochemistry Molecular Sequence Data Mutagenesis, Site-directed Polymerase Chain Reaction Genetics Structure-activity Relationship Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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