Women with rheumatoid arthritis performed 1 of 3 low intensity aerobic exercise protocols (15,25, and 35 minutes) 3 times per week for 12 weeks. A nontraining group served as controls. All exercise groups improved their aerobic capacity, exercise time, and joint counts. Subjects described improvement in activities of daily living and reduced joint pain and fatigue. Exercise duration up to 35 minutes can be therapeutic, and as little as 15 minutes of exercise 3 timedweek is sufficient to improve aerobic capacity in rheumatoid arthritis patients with severe limitations.

Microscopic study of normal synovial tissue from 16 humans of varying age disclosed an architectural pattern which did not vary significantly with age, sex or intra‐articular location. Except for fibrous synovium, the tissue samples were similar in vascularity, number of surface cell layers and in the differential composition of the surface cells. Histochemical procedures delineated a pericellular surface reticulin network but failed to establish the locus of hyaluronic acid synthesis.

Connective tissue activating peptides (CTAPs) extracted from leukocytes and platelets stimulate glycolysis and synthesis of glycosaminoglycan and DNA in cultured human connective tissue cells. CTAP-III, isolated from fresh or outdated human platelets, is a low molecular weight single-chain protein with an isoelectric point of 8.5 that markedly stimulates DNA synthesis and multiple aspects of glycosaminoglycan and proteoglycan metabolism. This report presents a definitive comparison of CTAP-III prepared by two methods [one designated (A), alternative] with similar platelet proteins described by others, beta-thromboglobulin (beta-TG) and low-affinity platelet factor 4 (LA-PF-4). CTAP-III, CTAP-III(A), LA-PF-4, and beta-TG have common antigenic determinants documented by immunoprecipitation and radioimmunoassay. CTAP-III, CTAP-III(A), and LA-PF-4 are biologically active in that they stimulate DNA and glycosaminoglycan synthesis by human synovial cells; beta-TG is inactive. Carboxyl-terminal digestion gave identical terminal sequences for CTAP-III, CTAP-III(A), and beta-TG. Amino-terminal sequence data indicate that CTAP-III and CTAP-III(A) (also LA-PF-4) are identical and differ from beta-TG only by an additional amino-terminal tetrapeptide (Asn-Leu-Ala-Lys-). The biologically active molecule, CTAP-III, may be proteolytically converted to its inactive degradation product (beta-TG) in the course of platelet aging, platelet storage, release from the platelets, or initiation of biological activity.

A patient population admitted to the hospital for either SLE or RA was surveyed for the subsequent development of neoplasms. The frequency of neoplasm in SLE patients appeared to be exaggerated, whereas the frequency of subsequent neoplasm in rheumatoid patients was unexpectedly low. A paucity of nephritis in the SLE group was noted. Further reports are encouraged so that the magnitude of the risk of malignancy developing with immunosuppressive therapy can be more precisely ascertained.Laboratory abnormalities suggesting that autoimmune mechanisms are responsible for some of the lesions seen with several of the connective tissue diseases have led to use of immunosuppressive drugs in the management of these disorders. Concern that such agents

This report describes a modification of a procedure developed by others for crosslinking IgG to protein A which itself is covalently linked to a gel support. Earlier immunoaffinity columns were described as having large antigen-binding capacities and stability under a variety of elution conditions. The present data show that columns constructed with earlier techniques were only partially stable to pH 3.0 buffers, and, as a result, bound less than 20% of the antigen predicted by theory. Modifying parameters of the dimethylpimelimidate crosslinking method led to immunoaffinity columns which did not leak immunoglobulin under low pH elution buffer conditions. The new immunoaffinity absorbants, because of the increased strength of the couple between the antibody and protein A, were capable of binding antigen at over 80% of their theoretical capacity.