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Gullberg, D.

Publications and source records attributed to Gullberg, D..

2 recordsLinked to original sources

Collagen-binding integrin alpha11beta1 contributes to joint destruction in arthritic hTNFtg mice

BackgroundIn rheumatoid arthritis (RA), fibroblast like synoviocytes (FLS) undergo a "tumor-like" transformation, wherein they develop an aggressive phenotype that is characterized by increased adhesion to components of cartilage extracellular matrix (ECM) and that contributes extensively to joint destruction. The collagen binding integrin 11{beta}1 was previously shown to be involved in similar processes in cancer-associated fibroblasts mediating tumorigenicity and metastasis in certain tumors. Therefore, this study aimed to study the role of integrin 11{beta}1 in RA and to characterize the effects of 11{beta}1 deficiency on the disease course and severity in arthritic hTNFtg mice. MethodsThe expression levels of integrin 11{beta}1 were analyzed by immunohistochemistry, immunofluorescence, and western blot analysis in synovial samples and FLS of patients with RA and osteoarthritis (OA) as well as in samples from wild type (wt) and arthritic hTNFtg mice. Furthermore, the subcellular expression of integrin 11{beta}1 was investigated in co-culture experiments with cartilage explants and analyzed by transmission electron microscopy. To investigate the effects of integrin 11{beta}1 deficiency, itga11-/- mice were interbred with hTNFtg mice and disease severity was assessed by clinical scoring of grip strength and paw swelling over the disease course. Hind paws of 12-weeks-old mice of all genotypes were analyzed by {micro}CT imaging followed by stainings of paraffin-embedded tissue sections with Toluidine-blue and tartrate-resistant acid phosphatase (TRAP) to evaluate established parameters of joint destruction such as inflammation area, cartilage destaining, FLS attachment to the cartilage surface, and bone damage. ResultsExpression levels of integrin 11{beta}1 were clearly elevated in synovial tissues and FLS from RA patients and hTNFtg mice, compared to the controls derived from OA patients and wt mice. Interestingly, this expression was shown to be particularly localized in focal adhesions of the FLS. As revealed by transmission electron microscopy, integrin 11{beta}1 expression was particularly evident in areas of direct cellular contact with the ECM of cartilage. Evaluations of clinical scorings and histomorphological analyses demonstrated that itga11-/-hTNFtg displayed alleviated clinical symptoms, higher bone volume, less cartilage destruction and reduced FLS attachment to the cartilage in comparison to hTNFtg mice. ConclusionsThe collagen-binding integrin 11{beta}1 is upregulated in the context of RA and its deficiency in mice with an inflammatory hTNFtg background leads to a significant reduction in the arthritic phenotype which makes integrin 11{beta}1 an interesting target for therapeutical intervention.

molecular biology↗

The endosome is a master regulator of plasma membrane collagen fibril assembly

Collagen-I fibrillogenesis is crucial to health and development, where dysregulation is a hallmark of fibroproliferative diseases. Here, we show that collagen-I fibril assembly required a functional endocytic system that recycles collagen-I to assemble new fibrils. Endogenous collagen production was not required for fibrillogenesis if exogenous collagen was available, but the circadian-regulated vacuolar protein sorting (VPS) 33b and collagen-binding integrin 11 subunit were crucial to fibrillogenesis. Cells lacking VPS33B secrete soluble collagen-I protomers but were deficient in fibril formation, thus secretion and assembly are separately controlled. Overexpression of VPS33B led to loss of fibril rhythmicity and over-abundance of fibrils, which was mediated through integrin 11{beta}1. Endocytic recycling of collagen-I was enhanced in human fibroblasts isolated from idiopathic pulmonary fibrosis, where VPS33B and integrin 11 subunit were overexpressed at the fibrogenic front; this correlation between VPS33B, integrin 11 subunit, and abnormal collagen deposition was also observed in samples from patients with chronic skin wounds. In conclusion, our study showed that circadian-regulated endocytic recycling is central to homeostatic assembly of collagen fibrils and is disrupted in diseases.

cell biology↗