Histochemical Localization of Acid Phosphatase in the Injured Rabbit Lens

Unakar, Nalin J.; Binder, Lester I.; Reddan, John R.

doi:10.1159/000264747

Cited by 14 publications

(4 citation statements)

References 5 publications

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“…Moreover, our current preoiminary data with cytochemical localization of acid phosphatase at the ultrastructural level in lenses undergoing both development and reversal of galactose induced cataracts suggests that lysosomal enzymes probably play a role in removal of debris through its breakdown. Our previous studies on mechanically injured rabbit lens ( Unakar et at., 1975) also implicated the role of lysosomal enzymes in lens repair. We suggest that in galactose-damaged lens, hydrolytic enzymes facilitate removal of tissue debris and thus contribute toward reestablihsment of transparence.…”

Section: Discussionmentioning

confidence: 99%

Scanning Electron Microscopy

Unakar¹,

Tsui²

1981

Ophthalmic Res

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Our laboratory undertook extensive light, transmission (TEM) and scanning elctron microscope (SEM) studies of rat lenses during the development and reversal phase of galactose-induced cataracts. These studies were undertaken in order to gain insight into the morphological manifestation of known biochemical changes that accompany development and reversal of galactose cataracts. In a recent report we presented TEM studies describing ultrastructural alterations associated with induction and reversal of galactose cataracts in rat lens. This report presents SEM findings of lenses undergoing such processes. Lenses of galactose and Purina Lab Chow-fed 50 g Sprague-Dawley rats were removed at desired times after initiation of diet and processed for SEM. When examined with SEM, some of the alterations induced with galactose included intercellular cyst formation, decrease in inter-digitations between fibers, abnormal configurations, conformation, granulation roughening and fragmentation of the lens fibers. These alterations progressed from equatorial regions to lens nucleus. Upon removal of galactose from the diet after the establishment of mature cataracts, normal lens fiber morphology was reestablished and the progression of normalization followed similar equator to nucleus pattern. However, lens damage and transparency was not restored throughout the lens even after 90 days following cessation of galactose when small nuclear opacity and damage was still evident. These observations compliment TEM findings reported previously from our laboratory. A probable mechanism for the reestablishment of lens transparency is proposed.

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Section: Discussionmentioning

confidence: 99%

Scanning Electron Microscopy

Unakar¹,

Tsui²

1981

Ophthalmic Res

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“…This limitation of artifacts caused by diffusion allows one to determine the site of acid phosphatase action more pre cisely. These differences in the results obtained with the two procedures used have been discussed in detail by Essner 1973], Our previous studies with a modified Gomori method demonstrated the presence of acid phosphatase in lens tissue at the ultrastructural level [Unakar et al, 1975], In this previous investigation, the presence of acid phosphatase in mechanically injured rabbit lens was demonstrated. In our subsequent study [Unakaret al, 1977], together with the one presented in this report, we have used two separate procedures for the ultrastructural localization of acid phosphatase (Gomori and Barka-Anderson proce dures) and demonstrated the presence of this enzyme in rat lens subjected to injury through galactose feeding.…”

Section: Discussionmentioning

confidence: 77%

“…Gorthy et al [1971] and Gorthy [1978] reported the presence of acid phosphatase and lysosomes in normal and cataractous lenses of aging rats. Previous reports from our laboratory [Unakar et al, 1975] demonstrated the presence of acid phosphatase and 'This study was supported by the National Eye Institute Research Grant EY-016R0 and was part of the Cooperative Cataract Research Group (CCRG) Program. lysosomes in rabbit lens epithelium following mechanical injury. Our pre liminary studies [Unakar et ah, 1977] also revealed the presence of acid phosphatase in the intercellular spaces of lens epithelium and superficial anterior cortical fibers in rat lenses during the initial phase of galactose alterations.…”

Section: Introductionmentioning

confidence: 99%

Acid Phosphatase

Nj¹,

Price²,

Tsui³

1982

Ophthalmic Res

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In the present investigation we have examined the presence, distribution and probable role of acid phosphatase in lenses of normal and galactose-fed rats. Acid phosphatase was localized in lenses using two separate cytochemical procedures (Gomori and Barka Anderson methods) and examined at the ultrastructural level. Both procedures, in general, provided similar sites of acid phosphatase activity, although with the Barka-Anderson method finer and larger amounts of well-defined reaction product were observable at the site of reaction. The reaction product was observed in lenses of both rats fed on regular laboratory chow and galactose-fed rats. The intracellular location of the reaction of this enzyme was primarily in lysosomes and occasionally in the endoplasmic reticulum cisternae. At the extracellular sites, it was near the epithelial cell membranes which abut each other and cortical fibers. However, in the cortical fibers the extracellular localization was at various sites on the entire intercellular space between neighboring fibers. The possible role of hydrolases in the lens tissue is discussed.

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“…Several investigators have suggested some pathologic role of lysosomal enzymes in aging and in cataracts (1,4,11,12,(15)(16)(17). Unaker et al (16,17) have reported that the ACPase activity increased during the induction of galactose cataracts and the Part of this study was presented at the thirtieth annual meeting of the Japan Society of Histochemistry and Cytochemistry held in Kyoto on October 23-25, 1989 (Tanaka, T., Sakai, M., Ihara, N. and Ogawa, K.: Localization of Acid Phosphatase Activity in the Lenses of ICR Rats).…”

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confidence: 99%