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Clinical Biochemistry of Domestic Animals (Sixth Edition) - UMK ...

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862<br />

Chapter | 28 Avian <strong>Clinical</strong> <strong>Biochemistry</strong><br />

deposition coincides with increased osteoblastic activity.<br />

When the bird starts to secrete the eggshell the medullary<br />

bone is resorbed by osteoclastic activity. Ca is deposited in<br />

the eggshell as Ca-carbonate and the P is excreted from the<br />

body. Medullary bone might be mistaken for a pathological<br />

condition when radiographs are being evaluated.<br />

D . Hypocalcemia Syndrome in African<br />

Grey Parrots<br />

In birds <strong>of</strong> prey and African grey parrots a hypocalcemia<br />

syndrome is known, characterized by hypocalcemic seizures.<br />

A striking feature <strong>of</strong> this syndrome in African grey parrots,<br />

which is not known in other birds, is that demineralization <strong>of</strong><br />

the skeleton is not obvious at the moment the seizures occur.<br />

The hypocalcemia syndrome is an important differential<br />

diagnosis in an African grey parrot that repeatedly falls <strong>of</strong><br />

its perch. Reference values for tCa concentrations in African<br />

grey parrots range from 2.0 to 3.25 mmol/L ( Rosskopf et al .,<br />

1982 ). Lumeij (1990) , studying a population <strong>of</strong> 72 African<br />

grey parrots found reference values <strong>of</strong> 2.1 to 2.6 mmol/L<br />

(inner limits <strong>of</strong> the percentiles P 2.5 to P 97.5 , with a probability<br />

<strong>of</strong> 90%) and a range from 2.0 to 3.4 mmol/L. Hochleithner<br />

(1989b) , studying 68 African grey parrots and using a dry<br />

chemistry system (Kodak Ektachem), reported reference<br />

values for Ca <strong>of</strong> 1.75 to 2.38 mmol/L (inner limits <strong>of</strong> the<br />

percentiles P 2.5 to P 97.5 ). Hochleithner (1989a) reported five<br />

cases <strong>of</strong> hypocalcemia in African grey parrots with plasma<br />

calcium concentrations ranging from 0.75 to 1.5 mmol/L.<br />

Rosskopf et al . (1985) stated that the one consistent finding<br />

<strong>of</strong> the hypocalcemia syndrome is a “ blood calcium level ”<br />

below 1.5 mmol/L. Values as low as 0.6 mmol/L have been<br />

reported ( Rosskopf et al ., 1985 ). When borderline calcium<br />

concentrations are found, the correction formula reported<br />

in Section VIII.A should be used. Stanford (2005) reported<br />

that 5/19 cases <strong>of</strong> hypocalcaemia in African grey parrots as<br />

diagnosed by low iCa concentrations had normal tCa concentrations<br />

and therefore concluded that measurement <strong>of</strong><br />

iCa concentration is vital to diagnose hypocalcaemia. This<br />

conclusion, however, was not supported by data on corrected<br />

tCa. With the current availability <strong>of</strong> ion selective electrodes,<br />

however, measurement <strong>of</strong> iCa seems to be the practical way<br />

<strong>of</strong> evaluating Ca status in birds. When timely treatment with<br />

parenteral Ca and vitamin D 3 preparations starts and sufficient<br />

dietary uptake <strong>of</strong> Ca is taken care <strong>of</strong>, clinical signs will<br />

regress in a short time. It is therefore likely that the disease<br />

is caused by Ca and vitamin D 3 deficiency. The higher incidence<br />

<strong>of</strong> the hypocalcaemia syndrome in African grey parrots<br />

might be related to the relatively higher dependence on<br />

ultraviolet light in this species ( Stanford, 2005, p. 136 ).<br />

E . Alkaline Phosphatase in Bone Disease<br />

Alkaline phosphatases (APs) form a group <strong>of</strong> membranebound<br />

glycoproteins that hydrolyze monophosphate esters<br />

at alkaline pH. Three different isoenzymes have been identified.<br />

Although there is a significant activity <strong>of</strong> AP in<br />

various tissues, the physiological role is unclear, except for<br />

AP in bone tissue. AP activity in bone reflects the activity<br />

<strong>of</strong> osteoblasts, and this enzyme is involved in the formation<br />

and mineralization <strong>of</strong> the bone matrix. In humans,<br />

increased AP activity is observed during growth and in<br />

osteoproliferative disorders ( Savova and Kirev, 1992 ).<br />

Different techniques have been used to identify fractions<br />

responsible for increased plasma activities. The heat<br />

inactivation test has been developed to distinguish AP activity<br />

<strong>of</strong> bone origin from that <strong>of</strong> liver origin ( Johnson et al .,<br />

1972 ; Posen et al ., 1965 ). In humans, residual activities after<br />

heat inactivation at 56°C higher than 35% indicate hepatic<br />

disease, whereas residual values lower than 25% indicate<br />

bone disease with increased osteoblastic activity ( Fennely<br />

et al ., 1969 ; Fitzgerald et al ., 1969 ; Stolbach, 1969 ). Using<br />

a guinea fowl model with bone tumors induced by osteopetrosis<br />

virus, Savova and Kirev (1992) were able to confirm<br />

these findings also for an avian species. They showed, by<br />

comparing the findings with the more sensitive wheat germ<br />

lectin method ( Brixen et al ., 1989 ; Rosalki and Foo, 1984 ),<br />

that for guinea fowl the AP activity <strong>of</strong> bone origin can be<br />

inactivated at 58°C rather than 56°C. Savova and Kirev<br />

(1992) found that AP activity <strong>of</strong> bone origin in 15-week-old<br />

guinea fowl was twice as high as that <strong>of</strong> 1-year-old birds.<br />

They also confirmed the positive correlation between the<br />

intensity <strong>of</strong> virus-induced excessive bone growth and serum<br />

AP activity reported previously by Sanger et al . (1986) and<br />

Barnes and Smith (1977) . The presumed high proportion <strong>of</strong><br />

AP <strong>of</strong> bone origin was supported by the low values <strong>of</strong> residual<br />

activity after heat inactivation at 58°C (14.7 3.7%) and<br />

after precipitation with wheat germ lectin (13 1.2%) during<br />

the period <strong>of</strong> active bone tumor formation ( Savova and<br />

Kirev, 1992 ).<br />

IX . DIABETES MELLITUS AND PLASMA<br />

GLUCOSE<br />

The basic metabolic regulation <strong>of</strong> glucose metabolism in<br />

birds is identical to that in mammals, but there is a quantitative<br />

difference. Reference values for plasma glucose in birds<br />

range somewhere between 11 and 25 mmol/L (Lumeij and<br />

Overduin, 1990 ; Rosskopf et al ., 1982 ). Physiological values<br />

up to 33 mmol/L have been observed postprandially in<br />

pigeons ( Lumeij, 1987b ). As a result <strong>of</strong> stress, plasma glucose<br />

concentrations up to 33 mmol/L may also be observed<br />

( Jenkins, 1994 ). The insulin content <strong>of</strong> the pancreas <strong>of</strong> granivorous<br />

birds is about one-sixth that <strong>of</strong> mammalian pancreata,<br />

whereas the glucagon content is about two to five times<br />

greater. Circulating plasma concentrations <strong>of</strong> glucagon (1 to<br />

4 ng/ml) are 10 to 50 times higher in birds than in mammals.<br />

Insulin is synthesized in the B cells <strong>of</strong> the pancreas, whereas<br />

glucagon is synthesized in the A cells.

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