Self-perpetuating arthritis was induced in knee joints of rabbits by intraarticular injections of large amounts of cell free extract derived from group A streptococci disintegrated mechanically. The pathological alterations were characterized by synovial lining cell proliferation, polymorphonuclear and mononuclear cell infiltration with the appearance of pseudo-follicles and pannus formation. Electron microscopical proliferation of B cells was predominant. An active inflammatory exudate and numerous new capillaries were also seen. The induced arthritis was self-perpetuating and appears to resemble human rheumatoid arthritis.
In previous reports (1, 2) it has been shown
that lysosomal enzymes derived from various
populations of mammalian leukocytes failed
to degrade 14C-Iabeled group A streptococci
in vitro, On the other hand, Staphylococcus
albus, Micrococcus Iysodeikticus and Escherichia
coli were degraded to a large extent by
leukocyte lysosomal enzymes. It was thus of
interest to study the degradation of a variety
of labeled microorganisms in vivo in inflammatory lesions in the thigh muscle of the
mouse induced by the injection of heat-killed
microorganisms. The results indicate that
there may be a correlation between the degree
of degradation of microorganisms by leukocyte
lysates in vitro (1, 2) and the length of
their persistence in lesion sites in vivo.
In previous reports (1-3), it has been shown
that lysosomal enzymes derived from a variety
of mammalian leukocyte populations degrade
14C-Iabeled Micrococcus lysodeikticus and
Staphylococcus albus extensively. On the other
hand, group A streptococci are very resistant
to lysis by leukocyte lysates. It has also been
shown that, unlike S. albus and M. lysodeikticus,
streptococci which are resistant to lysis
in vitro persist for long periods in granulomatous
lesions in mouse and rabbit tissues
(1, 2). Other reports (4, 5) have shown that
bacteria coated with specific antibodies are
degraded at a slower rate following phagocytosis,
as compared with untreated bacteria.
Cationic polyelectrolytes, such as polylysine
and polyarginine, agglutinate a variety of
bacteria (6), and cationic proteins derived
from leukocytes as well as from calf thymus
histone are bactericidal for a variety of microorganisms
(7). The possibility was therefore
investigated that, by analogy to antibodies,
cationic proteins may coat bacterial cells and
thus interfere with their degradation by leukocyte
lysosomal enzymes.
The distributions of vibrational, rotational and translational energies in the products of atom-diatomic molecule reactions are studied on the basis of their ``temperature parametere'. The validity of the vibrational temperature concept, which my characterize the variaous distributions, is examined from different points of view. The analysis is done on the basis of available data from chemiluminescence, chemical laser and molecular beams measurements and from classical trajectory calculations. All the reactions investigated are exothermic with exothermicities ranging between approximate to 17 kcal/mole and approximate to 85 kcal/mole. In most products a high degree of population inversion is found. An attempt is made to predict the complete vibrotational state distribution using the vibrational temperature only. This attempt is equivalent to the assumption that apart from the vibration, the other degrees of freedom have reached a (microcanonical) equilibrium. The agreement with experimental results is good.
Earlier reports had described the presence, in supernates of streptococcal steady-state cultures, of a macromolecular toxin which causes infiltrative and necrotic lesions in the heart and liver of rabbits and changes in the serum level of certain enzymes and lipids. In the present study, following treatment of the culture supernate concentrates with trichloroacetic acid and ethanol, and dialysis, material with these biologic activities has been found, in the dialysate, and was not excluded by Sephadex G-15. The molecular weight of the toxin, by this criterion, is near that of vitamin B12.
