Two types of receptors (DDR1 and DDR2) on cell surfaces get turned on when collagen binds to them, which then starts chains of chemical signals inside the cell that control growth and survival.
Scientific Claim
DDR1 and DDR2 receptor tyrosine kinases are activated by collagen binding, triggering downstream signaling pathways including MAPK and PI3K/Akt.
Original Statement
“Collagen binds to two types of DDRs including DDR1 (commonly expressed in epithelial cells) and DDR2 (commonly expressed in fibroblasts and mesenchymal cells) spontaneously at the extra/intracellular juxtamembrane domain, N-terminus, tyrosine kinase domain at the C-terminus and transmembrane domain. Collagen binding with the discoidin domain causes conformation changes in DDRs and tyrosine kinase domain phosphorylation, leading to the engagement of ShcA and Nck2 adapter proteins to the cytoplasmic domain of DDRs.”
Evidence Quality Assessment
Claim Status
appropriately stated
Study Design Support
Design supports claim
Appropriate Language Strength
definitive
Can make definitive causal claims
Assessment Explanation
The activation mechanism of DDRs by collagen is supported by multiple biochemical studies, justifying definitive language.
Evidence from Studies
Supporting (1)
The Molecular Interaction of Collagen with Cell Receptors for Biological Function