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Pharmaceuticals and Nutraceuticals from Fish Wastes and Their Activities
Published in Ramasamy Santhanam, Santhanam Ramesh, Subramanian Nivedhitha, Subbiah Balasundari, Pharmaceuticals and Nutraceuticals from Fish and Fish Wastes, 2022
Ramasamy Santhanam, Santhanam Ramesh, Subramanian Nivedhitha, Subbiah Balasundari
Types of collagen: The collagen of fish is of three types, namely, type I present in the skin, bone, and tendons; type II collagen in the cartilage tissue; and type III in the skin of young fish. The functional properties of these collagens largely depend on their amino acid composition, particularly in the concentrations of imino acids (proline and hydroxyproline). Generally, the collagen of warm water fishes such as bigeye-tuna and tilapia possess a higher imino acid level that of cold-water fishes, such as cod, whiting, and halibut (Eastoe and Leach, 1977).
Comparative Anatomy, Physiology, and Biochemistry of Mammalian Skin
Published in David W. Hobson, Dermal and Ocular Toxicology, 2020
Five types of collagen fibers have been described in the human. The difference between the types is based on amino acid composition and sequence. Type I collagen is found in the dermis, bone, tendons, ligament, and dentin. Type II collagen is found predominantly in hyaline cartilage. Type III is found in the fetal dermis, uterus, and cardiovascular system, and immunofluorescent studies show it to be localized in the papillary dermis. Type IV is found in the basal lamina.202–204 Type V collagen, also known as AB, is found in the cornea, dermis, placental membranes, and lung. This type of collagen is thought to be important in cell movement.205
Induction and Regulation of Arthritis by T Cell-Derived Collagen Binding Proteins
Published in Thomas F. Kresina, Monoclonal Antibodies, Cytokines, and Arthritis, 2020
This chapter describes the present knowledge and therapeutic potential for inflammatory arthritis of a unique set of proteins designated T cell-derived antigen binding molecules (TABM) or antigen-specific lymphokines or factors. The term TABM is used to assist in distinguishing these antigen binding proteins from conventional lymphokines or interleukins, which have no antigen uniqueness with regard to their generation or effector functions. Much of the content of this chapter deals with proteins that bind to type II collagen, as does collagenase. However, the T cell origin and lack of degradative activity clearly distinguish these collagen binding factors from members of the collagenase family of enzymes. To adequately discuss the potential therapeutic usefulness of collagen binding TABM, the review also provides an update on the increasing evidence that autoimmunity to type II collagen is pivotal for the expression of joint and eye inflammation in certain human connective tissue diseases. Because it could be critical for the understanding of inflammatory arthritis, the primary pathogenesis of collagen arthritis is also covered.
Reconstructive rhinoplasty using cadaver cartilage in relapsing polychondritis
Published in Baylor University Medical Center Proceedings, 2023
Rishabh Shah, Eugene L. Alford
Accumulating data strongly suggest that both humoral and cell-mediated immunity play a role in the pathogenesis of relapsing polychondritis. Antibodies to type II collagen, matrilin-1, and immune complexes are detected in the serum of patients. The possibility that an immune response to type II collagen may be important in the pathogenesis has been supported in animal studies. Humoral responses to type IX and type XI collagen, matrilin-1 (noncollagenous protein present in the extracellular matrix in cartilage), and cartilage oligomeric matrix protein have been demonstrated in some patients. One study showed that rats immunized with matrilin-1 were found to develop severe inspiratory stridor and swelling of the nasal septum. The rats had severe inflammation with erosions of the involved cartilage, which was characterized by increased numbers of CD4+ and CD8+ T cells in the lesions. All had IgG antibodies to matrilin-1. A subsequent study demonstrated serum anti-matrillin-1 antibodies in ∼13% of patients with relapsing polychondritis. Cell-mediated immunity may also be operative in causing tissue injury, since lymphocyte transformation can be demonstrated when lymphocytes of patients are exposed to cartilage extracts. T cells specific for type II collagen have been found in some patients, and CD4+ T cells have been observed at sites of cartilage inflammation.2
Significant Discrepancies in “Functional Characterization of Undenatured Type II Collagen Supplements: Are They Interchangeable?”: A Rejoinder
Published in Journal of Dietary Supplements, 2022
The article (1) concluded that the products were not interchangeable. We thank the authors for declaring their conflicts of interest and further rectifications including the mercury statement in the correction notice (2). The method used to analyze the content of undenatured type II collagen is an undisclosed proprietary ELISA-based method. The use of ELISA-based methods for undenatured type II collagen quantification is highly variable, as shown, for example, in Lugo 2019, (3) where different assay methods detected significantly different amounts of undenatured type II collagen for the same material tested. According to the ELISA-based method, negligible amounts of undenatured collagen were detected in CII-X samples. In contrast, using the methods of analysis based on the European Pharmacopeia (EP § 2.2.56), the content of undenatured type II collagen is 17% for CII-X, 10% for X1, and 23% for X2.
Severe osteoporosis in a premenopausal woman
Published in Scandinavian Journal of Rheumatology, 2019
Type II collagen provides strength to the structure and integrity of connective tissues such as muscles, joints, and skin. Collagen type II mutations are expressed in clinical syndromes called collagenopathies, which include achondrogenesis, spondyloepiphyseal dysplasia, Kniest dysplasia, and Stickler’s syndrome. Apart from severe osteoporosis and vertebral fractures, our patient did not express other characteristics of the above syndromes, such as facial deformities, short stature, deformed arms and legs, barrel-shaped chest, or hearing or visual losses. Given that the patient’s father had a history of severe osteoporosis and spontaneous fractures without an identifiable underlying cause, it is suspected that the patient’s pathology may be due to a genetic collagen defect transmitted from her father with an autosomal dominant trait. This phenotype of the collagen II mutation has not been previously correlated with only severe osteoporosis or osteogenesis imperfecta. We present this case to alert the medical community to the association of a collagen II mutation with severe osteoporosis in a young woman, without underlying causes such as alcoholism, heavy smoking, or endocrine, metabolic, or malabsorption disorders. The patient was placed on bisphosphonates (alendronate 35 mg/week), along with calcium and cholecalciferol supplementation to treat the severe osteoporosis.