Evidence for enhanced collagen type III deposition focally in the territorial matrix of osteoarthritic hip articular cartilage S. Hosseininia, M.A. Weis,

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Evidence for enhanced collagen type III deposition focally in the territorial matrix of osteoarthritic hip articular cartilage S. Hosseininia, M.A. Weis, J. Rai, L. Kim, S. Funk, L.E. Dahlberg, D.R. Eyre Osteoarthritis and Cartilage Volume 24, Issue 6, Pages 1029-1035 (June 2016) DOI: 10.1016/j.joca.2016.01.001 Copyright © 2016 Osteoarthritis Research Society International Terms and Conditions

Fig. 1 Western blot analysis of collagen type III degradation products in α-chymotrypsin extracts of OA and control femoral head cartilage samples (A). Extracts of full thickness tissue samples from individual hips were run on SDS-6%PAGE, blotted to PVDF membrane and Westerns developed using anti-type III collagen antibody (A) or stained with Coomassie blue to visualize total protein (B). Serum albumin is the only prominent protein by staining (confirmed by mass spectrometry) and is more prominent in the OA cartilage, presumably because of increased penetration from synovial fluid. Collagen type III N-propeptide trimers are consistently enriched in α-chymotrypsin extracts of OA cartilage compared with controls. Western blot analysis of collagen type II degradation products in chymotrypsin extracts of OA and control femoral head cartilage samples (C). A replicate SDS-6%PAGE gel to that shown in Fig. 1(A) was blotted to PVDF for Western development using mAb 1C10, which recognizes a sequence-specific epitope in the α1(II) chain. The main bands are essentially an intact α1(II) chain and large fragments of it. Osteoarthritis and Cartilage 2016 24, 1029-1035DOI: (10.1016/j.joca.2016.01.001) Copyright © 2016 Osteoarthritis Research Society International Terms and Conditions

Fig. 2 Electrophoretic resolution of pepsin-solubilized collagen types II and III from OA and control femoral head cartilage samples. SDS-6%PAGE was run using delayed DTT addition to separate α1(III) and α1(II) chain components. Protein was stained using Coomassie blue, revealing only type II and III collagen chains. Collagen type I is absent based on the lack of α2(I) which would run below α1(II). Osteoarthritis and Cartilage 2016 24, 1029-1035DOI: (10.1016/j.joca.2016.01.001) Copyright © 2016 Osteoarthritis Research Society International Terms and Conditions

Fig. 3 Immunohistochemical localization of collagen type III in full-thickness sections of femoral head cartilage from OA and fracture control hip joints. The mAb 4G9 was used as primary antibody to detect collagen III in full depth sections of frozen articular cartilage from OA and control joints. Representative sections from two OA samples, A (84 yr, female), B (62 yr, male) and two controls, C (59 yr, male), D (79 yr, female) are shown. Collagen type III is more prominent in cartilage from OA than control femoral heads consistent with the extracted collagen findings. In both it is most concentrated in territorial matrix surrounding cells in the upper half of the tissue. Osteoarthritis and Cartilage 2016 24, 1029-1035DOI: (10.1016/j.joca.2016.01.001) Copyright © 2016 Osteoarthritis Research Society International Terms and Conditions

Fig. 4 Illustrated molecular concept of polymeric pN type III collagen filaments deposited between and covalently attached to the surface of type II collagen fibrils (modified from reference8). Osteoarthritis and Cartilage 2016 24, 1029-1035DOI: (10.1016/j.joca.2016.01.001) Copyright © 2016 Osteoarthritis Research Society International Terms and Conditions