Hsp47, a collagen-specific molecular chaperone that localizes in the endoplasmic reticulum
(ER), is indispensable for molecular maturation of collagen. Hsp47, which is encoded by the …

Heat shock protein 47 (Hsp47) is an endoplasmic reticulum (ER)-resident molecular
chaperone essential for correct folding of procollagen in mammalian cells. In this Review …

Extracellular matrix (ECM) proteins are biosynthesized in the rough endoplasmic reticulum
(rER) and transported via the Golgi apparatus to the extracellular space. The coat protein …

Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue, and these
distinct hydroxylation patterns modulate collagen cross‐linking to generate a unique …

In macroautophagy, membrane structures called autophagosomes engulf substrates and
deliver them for lysosomal degradation. Autophagosomes enwrap a variety of targets with …

The collagenopathies are a diverse group of diseases caused primarily by mutations in
collagen genes. The resulting disruptions in collagen biogenesis can impair development …

Chaperonopathies are caused by qualitatively and/or quantitatively abnormal molecular
chaperones. These are proteins, chaperoning system components along with co …

This article describes several recent examples of miRNA governing the regulation of the
gene expression involved in bone matrix construction. We present the impact of miRNA on …

Cystic Fibrosis (CF) is a recessively inherited disease caused by mutations in the Cystic
Fibrosis Transmembrane Conductance Regulator (CFTR) gene. CFTR has a pivotal role in …

Heat shock protein 47 (HSP47), encoded by the SERPINH1 gene, is a molecular chaperone
essential for correct folding of collagens. We report a homozygous p.(R222S) substitution in …