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beta-Lactoglobulin and ovalbumin in mature human milk in healthy lactating Japanese women (n = 24) were determined by using an enzyme-linked immunosorbent assay. Subjects consumed > or = +200 mL cow milk/d for 1 wk before the sampling day and exactly 200 mL cow milk on the morning of the sampling day. beta-Lactoglobulin was detected (> 0.1 microgram/L) in breast milk in 15 of the 24 subjects (62.5%), with a maximum concentration of 16.5 micrograms/L. Ovalbumin was detected in only two subjects (8.3%) after the subjects followed their usual diet. beta-Lactoglobulin concentrations were low in the subjects whose cow milk consumption during the entire lactating period was low, even though all subjects consumed the same amount of cow milk before sampling. This result suggests that beta-lactoglobulin concentrations in breast milk are related to long-term consumption of cow milk. Amounts of food antigens in breast milk may be controlled by modifying the daily maternal diet.

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SummaryA new type of substitution, Arg to Ser at γ275, has been found in a heterozygous dysfibrinogen derived from a 23-year-old woman with no major bleeding or thrombosis. By sequence analyses of the affected γ-chain and its gene, we found a single amino acid substitution of γ Arg-275 to Ser in an aberrant γ (274-302) residue peptide isolated from lysyl endopeptidase-digests of the patient’s fibrinogen. In agreement with this amino acid substitution, we identified a single nucleotide exchange of A for C at position 5728 in the γ-chain gene creating a codon (AGC) encoding Ser instead of the codon (CGC) encoding Arg at position γ 275. Like two other known types of mutants with a His or Cys substitution at this position, the functional abnormality was characterized by delayed fibrin polymerization, most likely due to impaired abutting of two D domains of adjacent fibrin monomers in the same strand of fibrin protofibrils. The structural derangement that affects the D:D association may not be so severe as compared with those of Cys and His mutants, possessing an additional disulfide-linked Cys molecule and an imidazole ring at the mutation site, respectively.

A new type of gamma Gly-268 (GGA) to Glu (GAA) substitution has been identified in a homozygous dysfibrinogen by analyses of the affected polypeptide and its encoding gene derived from a 58 year-old man manifesting no major bleeding or thrombosis. The functional abnormality was characterized by impaired fibrin assembly most likely due to failure to construct properly aligned double-stranded fibrin protofibrils. This presumption was deduced from the following findings: (1) Factor XIIIa-catalyzed cross-linking of the fibrin gamma-chains progressed in a normal fashion, indicating that the contact between the central E domain of one fibrin monomer and the D domain of another took place normally; (2) Nevertheless, factor XIIIa-catalyzed cross-linking of the fibrinogen gamma-chains was obviously delayed, suggesting that longitudinal association of D domains of different fibrin monomers, ie, D:D association was perturbed; (3) Plasminogen activation catalyzed by tissue-type plasminogen activator was not as efficiently facilitated by polymerizing fibrin monomer derived from the patient as by the normal counterpart. Therefore, gamma Gly-268 would not be involved in the 'a' site residing in the D domain, which functions as a complementary binding site with the thrombin-activated 'A' site in the central E domain, but would be rather involved in the D:D self association sites recently proposed for human fibrinogen. Thus, the gamma Glu-268 substitution newly identified in this homozygous dysfibrinogen seems to impair proper alignment of adjacent D domains of neighboring fibrin molecules in the double-stranded fibrin protofibril, resulting in delayed fibrin gel formation.

SummaryWe have studied the expression of plasminogen activator inhibitor 2 (PAI-2) in the adult mouse and during embryonic development using immunohistochemistry and the polymerase-chain reaction. Mouse PAI-2 mRNA was mainly expressed in the skin, bone-marrow, spleen, lung, thymus, and urinary bladder. Immunohistochemical studies suggested that PAI-2 was synthesized in macrophages and epithelial cells such as skin epithelial cells, transitional cells of the urinary bladder, and mesothelial cell of peritoneum and pleura. PAI-2 mRNA and antigen expression was observed only in the skin of 15 day-old mouse embryos. These data suggest that PAI-2 may play a role in protecting the mouse embryo from the protease attack in the amniotic fluid and also in maintaining and/or protecting the structure of various surfaces in the mouse.

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We describe the relations between primary brain stem or cerebellar infarct or haemorrhage and secondary inferior olivary pseudo-hypertrophy (OPH). We identified 17 patients (43.6%) among 39 with brain stem or cerebellar vascular disease who had MRI follow-up more than 3 months after their ictus, with OPH. The primary lesions in the 22 cases without OPH were 11 haemorrhages, including 8 medial cerebellar and 3 brain stem lesions, and 11 infarcts: 4 brain stem lesions without accompanying cerebellar involvement, 2 cerebellar infarcts with brain stem extension, and 5 cerebellar lesions without a brain stem infarct. The causative lesion in the 17 patients with OPH included 5 brain stem and 7 cerebellar haemorrhages and 5 brain stem infarcts; no cerebellar infarcts without brain stem involvement were found to cause OPH. Primary involvement of the tegmentum of the brain stem was closely related to secondary OPH, but we could not characterise MRI differences in the cerebellar lesions between the patients with or without OPH.