Biomedical evaluation of Verreaux's sifaka (Propithecus verreauxi) from Kirindy Mitea National Park in Madagascar.

Evaluation of the health, prevalence, and incidence of diseases in wild populations is a critical component of wildlife management. In addition, the establishment of reference physiologic parameters can Verreaux's sifaka (Propithecus verreauxi) from Kirindy Mitea National Park, Madagascar, during two field captures incontribute to the assessment of population risks. Complete medical evaluations were performed on 33 wild June 2010 and June 2011. Each animal received a complete physical examination: weight, body temperature, heart rate, and respiratory rate were recorded, and ectoparasites collected. Blood samples were collected for complete blood cell count, differential white blood cell count, hemoparasite examination, serum biochemical profile, fat-soluble vitamin analysis, trace mineral analysis, and toxoplasmosis and viral serology. Fecal samples were collected for bacterial culture and endoparasite examination. Significant differences exist between age classes for neutrophil and lymphocyte count, alkaline phosphatase, and creatinine values. Parasites detected were Callistoura sp., Bertiella lemuriformis, and Dipetalonema petteri. This publication reports the first complete biomedical evaluation of the P. verreauxi and provides a basis for hematologic and biochemical comparisons of P. verreauxi in the wild.

Effects of anthropogenic disturbance on indri (Indri indri) health in Madagascar.

Anthropogenic habitat disturbance impairs ecosystem health by fragmenting forested areas, introducing environmental contamination, and reducing the quality of habitat resources. The effect of this disturbance on wildlife health is of particular concern in Madagascar, one of the world's biodiversity hotspots, where anthropogenic pressures on the environment remain high. Despite the conservation importance of threatened lemur populations in Madagascar, few data exist on the effects of anthropogenic disturbance on lemur health. To examine these impacts, indri (Indri indri) populations were evaluated from two forest reserves that differ in their exposure to anthropogenic disturbance. We compared the health status of 36 indri individuals from two sites: one population from a protected, undisturbed area of lowland evergreen humid forest and the other population from a reserve exposed to frequent tourism and forest degradation. Comparison of indri health parameters between sites suggests an impact of anthropogenic disturbance, including significant differences in leukocyte count and differential, 12 serum parameters, 6 trace minerals, and a higher diversity of parasites, with a significant difference in the presence of the louse, Trichophilopterus babakotophilus. These data suggest that indri living in disturbed forests may experience physiological changes and increased susceptibility to parasitism, which may ultimately impair reproductive success and survival.

Red cell polymorphisms in nonhuman primates: a review.

Development as well as current status of the knowledge of nonhuman primate blood groups are discussed together with some practical implications of the red cell antigen polymorphisms in anthropoid apes, Old and New World monkeys and prosimians. Recent data on molecular biology and genetics throw light on the relationships among simian and human red cell antigens and their evolutionary pathways.

[Study of equivalents of rhesus antigens in non-human primates]. / Etude des équivalents des antigènes Rhésus chez les primates non hominiens.

Human alloantibodies specific of some Rh antigens cross-react with non human primates red blood cells. These crossreactions demonstrated that only African apes express equivalents of Rho (D) and hr' (c). The antigenic resemblance between these two human antigens and their primate homologues is confirmed by the reactivities of human anti-D and anti-c monoclonal antibodies. The use of a human Rh cDNA probe allowed to confirm by Southern blot hybridization that nonhuman primates possess Rh-like genes. The number of Rh-like genes per haploid genome was deduced from the results obtained with exon-specific probes.

Prosimian hemoglobins--V. The primary structures of the alpha-I, alpha-II and beta-hemoglobin chains of Hapalemur griseus, with a note on the classification of Microcebus.

1. The duplicated adult hemoglobins were isolated from a mature Hapalemur griseus and the constituent chains prepared. Sequence analysis of the isolated alpha-globins showed that the alpha-I and alpha-II chains differed by a glycine for lysine substitution at position 15. 2. The complete amino acid sequence of the single adult beta-globin of Hapalemur griseus was determined. The beta-globin sequence of Hapalemur griseus clusters with those of other authentic lemurs, and is clearly separated from the sequences characteristic of lorisiform primates. 3. Partial sequence analysis of the beta-globin of Microcebus murinus showed only a single amino acid difference when compared to the Hapalemur globin. 4. Partial sequence analysis of the alpha-globin of Microcebus murinus showed only three amino acid residues that are not found in other lemuriform alpha-globins; two of these are unique to Microcebus among all known prosimian alpha-globin sequences. 5. The Microcebus alpha- and beta-globins are more similar to the homologous lemuriform sequences than they are to lorisiform sequences.

Cortisol levels, binding, and properties of corticosteroid-binding globulin in the serum of primates.

New World primates have exceptionally high plasma levels of cortisol and other steroid hormones when compared with humans and other primates. It has been suggested that this difference can be explained by either low affinity or concentration of cellular steroid receptors. We have assessed cortisol availability in serum from several species of New and Old World primates under physiological conditions (whole serum at 37 degrees C). Measurements were made of total and free cortisol, corticosteroid-binding globulin (CBG) binding capacity and affinity for cortisol, distribution of cortisol in serum, and its binding to albumin. In agreement with earlier reports, plasma free cortisol levels in Old World primates, prosimians, and humans range from 10-300 nM. However, very high total plasma cortisol together with low CBG binding capacity and affinity result in free cortisol concentrations of 1-4 microM in some New World primates (squirrel monkey and marmosets) but not in others such as the titi and capuchin. In squirrel monkeys, free cortisol levels are far greater than might be predicted from the affinity of the glucocorticoid receptor estimated in cultured skin fibroblasts. In addition to low affinity, CBG from squirrel monkeys and other New World primates exhibits differences in electrophoretic mobility and sedimentation behavior in sucrose density ultracentrifugation, suggestive of a molecular weight that is approximately twice that of CBG from other species. Together with other data these results indicate that the apparent glucocorticoid resistance found in New World primates is a complex phenomenon that is not easily explained by present concepts of glucocorticoid action.

Plasma cortisol transport and primate evolution.

Primates have diverged into three major evolutionary groups: prosimians, Old World primates, and New World primates; the last group is distinguished by high circulating cortisol concentrations and resistance to the action of glucocorticoids. We have studied a large spectrum of primate species within these groups to characterize the phylogenetic relationships of cortisol-binding globulin (CBG) among them. The CBG in each species was found to be glycosylated, as judged from lectin interactions, and to exhibit an electrophoretic mobility similar to that of human CBG. Although the CBG affinity for cortisol differed among species, the effects of changes in temperature on the CBG affinity were similar. Strikingly, the CBG-binding capacity of plasma in the New World primates was 1/10th to 1/100th those in the Old World primates and prosimians, while the CBG-binding affinity for cortisol was lower. The reduced capacity and affinity of CBG result in a markedly higher fraction of unbound plasma cortisol in the New World primates than in the Old World primates or the prosimian species examined. This evolutionary pattern of CBG may be a compensatory mechanism for the target organ resistance to glucocorticoids that characterizes the New World monkeys.

Hematology of the lesser mouse lemur (Microcebus murinus). A preliminary study.

Some blood values of 86 lesser mouse lemurs (Microcebus murinus) maintained in captivity are presented. These are comparable with those of other prosimians: PCV 51.7%, RBC 9.2 X 10(6)/mm3, MCV 57.5 micron3, WBC 12,900/mm3, lymphocytes 59.7%, neutrophils 30.7%, monocytes 4.8%, eosinophils 4.2%, basophils 0.6%. We noted no significant difference between the sexes except that the percentage of lymphocytes was slightly lower in the females (with a corresponding percentage of neutrophils slightly higher). The lymphocyte:neutrophil ratio decreases with age, particularly in young animals; the hematocrit does not vary in adults.

Amino acid sequences of the alpha and beta chains of adult hemoglobin of the brown lemur, Lemur fulvus fulvus.

Globin prepared from hemoglobin of the brown lemur (Lemur fulvus fulvus) was separated into alpha and beta chains by chromatography on a CM 52 column. The S-aminoethylated alpha and beta chains were each digested with trypsin and resulting peptides were isolated. The amino acid sequences of the tryptic peptides were established. The ordering of these peptides in the alpha and beta chains was deduced from the homology of their amino acid sequences with that of human adult hemoglobin. The primary structure of brown lemur hemoglobin thus obtained differs from that of human hemoglobin in 15 amino acids in the alpha chain and 26 in the beta chain.

Amino acid sequences of the alpha and beta chains of adult hemoglobin of the slender loris, Loris tardigradus.

alpha and beta chains from adult hemoglobin of the slender loris (Loris tardigradus) were isolated by Amberlite CG-50 column chromatography. After S-aminoethylation, both chains were digested with trypsin and the amino acid sequences of the tryptic peptides obtained were analyzed. Further, the order of these tryptic peptides in each chain was deduced from their homology with the primary structures of alpha and beta chains of human adult hemoglobin. Comparing the primary structures of the alpha and beta chains of adult hemoglobin of the slender loris thus obtained with those of adult hemoglobin of the slow loris, 4 amino acid substitutions in the alpha chains and 2 in the beta chains were recognized.

Amino acid sequences of the aplpha and beta chains of adult hemoglobin of the tupai, Tupaia glis.

Globin prepared from hemoglobin of adult tupai (Tupaia glis) was separated into alpha and beta polypeptide chains by CM-cellulose column chromatography. The S-aminoethylated alpha polypeptide chain and S-carboxymethylated beta polypeptide chain were each digested with trypsin, and the sequences of all the peptides thus obtained were established. The ordering of these tryptic peptides in the alpha and beta polypeptide chains was deduced from the homology of their primary structures with that of human adult hemoglobin. In this way the primary structures of the alpha and beta polypeptide chains of tupai hemoglobin were established; 27 amino acids in the alpha polypeptide chain and 26 in the beta chain differ from those in human adult hemoglobin.

Chromosomes of lemuriformes. II. Chromosome polymorphism in Lemur fulvus collaris (E. Geoffroy 1812).

Two previously unreported diploid numbers, 2N = 50 and 2N = 51, from five individual Lemur fulvus collaris are described. In both chromosome complements, the nombre fondamental is 64. The 2N = 50 complement is composed of 7 pairs of bi-armed chromosomes, 17 pairs of acrocentric chromosomes with small short arms, and acrocentric sex chromosomes. The 2N = 51 complement is identical with these exceptions: Only one member equivalent to bi-armed pair 6 of L.f. collaris (2N = 50) is present, and two extra acrocentrics are found in the 2N = 51 complement. G-banding analyses suggest that these chromosomes are a heteromorphic pair of the Robertsonian type. This conculsion is supported by evidence from studies of meiotic pairing relationships of the three chromosomes and the complements of hybrids resulting from interspecific matings. Comparison of the 2N = 50 and 2N = 51 complements with a published 2N = 48 complement suggests that these new karyotypes do not provide a lineal link between the 2N = 52 and 2N = 48 karyotypes (Rumpler, Y., and R. Albignac 1969 C.R. Soc. Biol., 163: 1989-1992).