MeSH Browser

MeSH Heading: Complement C1r
Tree Number(s): D08.811.277.300.280; D12.776.124.486.274.045.280; D12.776.124.486.274.050.280
Unique ID: D015923
RDF Unique Identifier: http://id.nlm.nih.gov/mesh/D015923
Scope Note: A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.
Entry Term(s): C1r Complement; Complement 1r; Complement Component 1r
Pharm Action: Immunologic Factors
Registry Numbers: EC 3.4.21.41
Previous Indexing: Complement 1 (1979-1989); Complement Activating Enzymes (1979-1989); Enzyme Precursors (1979-1982)
Public MeSH Note: 2006; see COMPLEMENT 1R 1990-2005
History Note: 2006 (1990)
Date Established: 1990/01/01
Date of Entry: 1989/05/25
Revision Date: 2006/07/05

Allowable Qualifiers: administration & dosage (AD)

adverse effects (AE)

agonists (AG)

analysis (AN)

antagonists & inhibitors (AI)

biosynthesis (BI)

cerebrospinal fluid (CF)

chemical synthesis (CS)

chemistry (CH)

classification (CL)

deficiency (DF)

drug effects (DE)

economics (EC)

genetics (GE)

history (HI)

immunology (IM)

isolation & purification (IP)

metabolism (ME)

pharmacokinetics (PK)

pharmacology (PD)

physiology (PH)

poisoning (PO)

radiation effects (RE)

standards (ST)

supply & distribution (SD)

therapeutic use (TU)

toxicity (TO)

ultrastructure (UL)

urine (UR)

Concept UI: M0024367
Registry Numbers: EC 3.4.21.41
Scope Note: A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.
Terms: Complement C1r Preferred Term
Term UI T622152
Date12/06/2004
LexicalTag NON
ThesaurusID NLM (2006); Complement Component 1r
Term UI T622153
Date12/06/2004
LexicalTag NON
ThesaurusID NLM (2006); C1r Complement
Term UI T631372
Date02/23/2005
LexicalTag NON
ThesaurusID NLM (2006); Complement 1r
Term UI T047240
Date01/01/1999
LexicalTag NON
ThesaurusID NLM (1990)

Complement C1r MeSH Descriptor Data 2025