Biomedical subjects

K Akasaki

Publications and source records attributed to K Akasaki.

At least 19 recordsLinked to original sources

PubMed1998

Immunochemical distinction of Aloe vera, A. arborescens, and A. chinensis gels.

Verectin antiserum raised in white rabbits was immunoprecipitated with the Aloe vera nondialysable fraction. Analysis of the immunoprecipitation revealed that verectin accounted for about 1.25% of the total proteins in the nondialysable fraction of Aloe vera gel. The verectin antibody showed differential immunoreactivities against nondialysable fractions of A. arborescens, A. chinensis, and A. vera: 1) an immunopreciptin line was formed against the fraction of A. vera, but not against those of A. arborescens and A. chinensis gel in an Ouchterlony double immunodiffusion test and 2) an immunopositive band was detected in the A. vera and A. chinensis nondialysable fractions but not in that of A. arborescens in immunoblotting. These findings indicate that the verectin antibody can be used to distinguish Aloe materials.

Animals↗

PubMed1997

Identification and characterization of a major lysosomal membrane glycoprotein, LGP85/LIMP II in mouse liver.

We previously have purified and characterized a major lysosomal membrane glycoprotein termed LGP85 (LIMP II) in rat liver lysosomes. In this study, LGP85 in mouse liver lysosomes was identified and characterized by biochemical and molecular biological methods. Lysosomal membranes were isolated from murine liver by differential centrifugation. LGP85 was present in the lysosomal membrane fraction from mouse liver in a comparable amount to another lysosomal membrane glycoprotein, lamp-2. Mouse LGP85 (M-LGP85) from liver lysosomal membranes exhibited an Mr of 80,000 on SDS-PAGE, which is smaller by 5,000 than that of rat LGP85 (R-LGP85). M-LGP85 was immunochemically detected in the extracts of brain, heart, lung, liver, and kidney. A cDNA encoding M-LGP85 was cloned from mouse liver cDNA library. The primary protein structure deduced from a nucleotide sequence of M-LGP85 cDNA indicated that M-LGP85 consists of 478 amino acids with Mr of 54,069. M-LGP85 showed 93.3 and 86.0% sequence similarities to its rat and human counterparts in amino acids, respectively. M-LGP85 contains 11 potential N-glycosylation sites which are heavily glycosylated, resulting in the increased Mr of M-LGP85 present in the mouse liver lysosomes. It is likely that M-LGP85 traverses the lysosomal membrane twice, with an NH2-terminal transmembrane domain, and another hydrophobic domain near the COOH-terminus. M-LGP85 has a protruding COOH-terminal cytoplasmic tail consisting of amino acid residues including the leucine-isoleucine sequence shown to be the lysosomal targeting signal of R-LGP85 and human LGP85 (H-LGP85). The high level of expression of M-LGP85 in the lysosomal membrane, the high structural similarities among M-, R-, and H-LGP85, and the occurrence of M-LGP85 in all the mouse tissues examined suggest the essential and constitutive function of LGP85 in lysosomes.

Amino Acid Sequence↗

PubMed1996

Biosynthetic transport of a major lysosome-associated membrane glycoprotein 2, lamp-2: a significant fraction of newly synthesized lamp-2 is delivered to lysosomes by way of early endosomes.

Lysosomal membranes contain two highly glycosylated proteins, designated as lamp-1 and lamp-2, as major components. Lamp-1 and lamp-2 are similar to each other in the protein structure. Here, we investigated the biosynthetic transport of lamp-2 through the endocytic vacuoles in cultured rat hepatocytes in comparison with that of lamp-1, which has previously been studied [Akasaki et al. (1995) Exp. Cell Res. 220, 464-473]. Newly synthesized lamp-2 (NS-lamp-2) was transported to the trans-Golgi from rough endoplasmic reticulum with a half time (t1/2) of 32 min, more slowly than NS-lamp-1 (t1/2 = 13 min). After leaving the trans-Golgi, NS-lamp-2 is transferred to at least three compartments; the cell surface (t1/2 = 47 min), cell peripheral early endosomes (t1/2 = 38 min) and perinuclear late endosomes (t1/2 = 48 min). NS-lamp-2 transported to any compartment is delivered finally to lysosomes (t1/2 = 90 min). A significant fraction of NS-lamp-2 (45% of the total) was transported from the trans-Golgi to early endosomes, and then delivered to dense lysosomes via perinuclear late endosomes, whereas a major portion of NS-lamp-1 follows an intracellular route to late endosomes without passing through the cell periphery. NS-lamp-2 leaves the cell peripheral region more rapidly than NS-lamp-1. The kinetic and quantitative data for biosynthetic transport of NS-lamp-2 to early endosomes and the cell surface indicate that NS-lamp-2 may be transported first to early endosomes, from which a small portion of it (approximately 3.5% of the total) moves to the plasma membrane via a recycling system. In contrast, a small fraction of NS-lamp-1 is transported to the plasma membrane directly from the trans-Golgi, since NS-lamp-1 is delivered to the plasma membrane and early endosomes with almost the same half times.

Animals↗

PubMed1995

Biosynthetic transport of a major lysosomal membrane glycoprotein, lamp-1: convergence of biosynthetic and endocytic pathways occurs at three distinctive points.

We studied the kinetics of the biosynthetic transport of lysosome-associated membrane glycoprotein-1 (lamp-1) to the endocytic compartments in cultured rat hepatocytes. Newly synthesized lamp-1 (NS-lamp-1) was transported to the trans-Golgi from rough endoplasmic reticulum with a half time (t1/2) of 13 min. From the trans-Golgi, at least 25% of NS-lamp-1 was delivered to the cell periphery: to the cell surface and early endosomes with t1/2 s of 32 and 33 min, respectively. A comparison of the kinetics of the biosynthetic transport of lamp-1 to both compartments demonstrated that NS-lamp-1 takes two peripheral routes from the Golgi apparatus; it is delivered to early endosomes directly and after reaching the cell surface. A major portion of NS-lamp-1 follows a direct intracellular pathway to late endosomes (t1/2 = 45 min) and subsequently to lysosomes (t1/2 = 85 min). The kinetic data of the biosynthetic transport to these endocytic vacuoles suggested that a significant fraction of NS-lamp-1 returns to the late endosomes immediately after its arrival at lysosomes and that there is a unique retrograde delivery of NS-lamp-1 from late to early endosomes prior to its transport to lysosomes. Thus, in cultured rat hepatocytes, the lamp-1 biosynthetic and the endocytic pathways converge at the three distinctive points. Late endosomes are centrally situated in the complex biosynthetic route of lamp-1.

Animals↗

PubMed1995

Purification and characterization of a major kyotorphin-hydrolyzing peptidase of rat brain.

We purified a major kyotorphin (L-Tyr-L-Arg)-hydrolyzing peptidase (KTPase) from the rat brain, to electrophoretic homogeneity using conventional chromatographic techniques. KTPase was purified 1,660-fold with a specific activity of 161 mumol/min/mg protein and 6.8% recovery. The purified enzyme was composed of a single polypeptide with a molecular mass of 67 kDa and an isoelectric point (pI) of 5.5. KTPase has the ability to hydrolyze a variety of natural dipeptides. It also liberated NH2-terminal tyrosine from Tyr-Gly-Gly and Tyr-Tyr-Leu. Bestatin and arphamenine B were potent inhibitors of this enzyme, while amastatin and puromycin had little effect. An excess of anti-KTPase antibody raised in a white rabbit precipitated approximately 80% of the kyotorphin-hydrolyzing activity in the cytosol of rat brain. These data suggested that 67 kDa KTPase has a role in the degradation of kyotorphin within neuronal cells of the rat brain.

Amino Acid Sequence↗

PubMed1994

Identification and characterization of lysosomal enzymes involved in the proteolysis of phenobarbital-inducible cytochrome P450.

We have studied lysosomal proteases capable of degrading a major form of cytochrome P450 (CYP2B1) which was purified from the liver microsomes of phenobarbital-treated rats. After incubation of CYP2B1 with extracts of triton-filled lysosomes (tritosomes), its proteolysis was measured by a quantitative immunoblot procedure. A CYP2B1 protein band with an apparent molecular mass of 53 kilodaltons (kDa) was degraded to 42-, 38-, and 29-kDa polypeptides after a short period of incubation. These proteolytic fragments disappeared on prolonged incubation. One milligram of tritosomal protein contained enough activity to hydrolyze approximately 67.3 micrograms CYP2B1 protein/min at pH 4.5. Approximately 85% of the hydrolyzing activity was localized in a soluble fraction of the tritosomes. The degradation of CYP2B1 was effectively inhibited by pepstatin A, an aspartic protease inhibitor, but not by phenylmethanesulfonyl fluoride (PMSF), o-phenanthroline and leupeptin. CYP2B1-hydrolyzing activity was coeluted with cathepsin D when the soluble fraction was chromatographed by means of Ultrogel Ac44 gel filtration. Cathepsin D, purified from rat livers, was able to degrade CYP2B1 at pH 4.5 which corresponds to the intralysosomal pH. These results indicate that cathepsin D is responsible for the major CYP2B1-hydrolyzing enzyme activity in lysosomes.

Amino Acid Sequence↗

PubMed1994

Cycling of an 85-kDa lysosomal membrane glycoprotein between the cell surface and lysosomes in cultured rat hepatocytes.

We studied the endocytic transport of an 85-kDa lysosomal membrane glycoprotein (LGP85) from the cell surface to lysosomes in cultured rat hepatocytes. Fab' fragments of a monoclonal antibody against LGP85 (YA30 mAb) were conjugated with horseradish peroxidase (HRP) and then used as probes to monitor the endocytic transport of LGP85 from the plasma membrane to lysosomes. Continuous internalization and lysosomal transport of HRP-YA30 mAb Fab' occurred in the hepatic cells, resulting in its accumulation in the dense lysosomal fraction obtained from the cells on Percoll density centrifugation. The endocytic transport of HRP-YA30 mAb continued in the presence of the protein synthesis inhibitor, cycloheximide, indicating that LGP85 is cycled between the cell surface and lysosomes or endosomes, like other lysosomal membrane glycoproteins, lamp-1 and lamp-2, as reported previously [Akasaki et al. (1993) J. Biochem. 114, 598-604]. The half times (t1/2) of internalization and lysosomal transport of LGP85 were 32 min and 2.0 h, respectively. The kinetics of endocytic transport for LGP85 are very similar to those of lamp-1 and lamp-2. LGP85 possesses a short cytoplasmic tail whose amino acid sequence is quite different from those of lamp-1 and lamp-2. Therefore, these results suggested that continuous internalization from the cell surface and lysosomal transport of of endogenous LGP85 occur through a mechanism that can recognize this novel amino acid sequence, probably a Leu-Ile-containing motif, in normal hepatic cells of rat.

Amino Acid Sequence↗

PubMed1993

Detection of subtle differences in the surface structure of lysozymes by use of an immobilized Fab fragment.

A method was developed to evaluate the association constant at physiological pH (pH 7.5) between a lysozyme and the Fab fragment derived from anti-lysozyme monoclonal antibody 37-7, which was immobilized to the adsorbent for HPLC. Comparison of the association constants between lysozymes and the immobilized Fab fragment indicated that mAb 37-7 recognized the prominently exposed regions (hills and ridges) around His15 of hen lysozyme, but His15 itself was not directly involved in the binding with mAb 37-7. Moreover, the epitope was confirmed by the reactivity of His15 with monoiodoacetic acid in the presence of mAb 37-7. The association constant of 15-carboxymethylated histidine lysozyme (15CM lysozyme) with the immobilized Fab fragment was smaller by one-seventh than that of 15-carboxamidated histidine lysozyme, though the side chains introduced were almost identical in size. From the pH titration of 15CM lysozyme with 13C-enriched carboxyl group by use of 13C-NMR, the pKa of the introduced carboxyl group was evaluated to be 5.06. Since the carboxyl group was fully ionized under the conditions of measurement (pH 7.5), electrostatic repulsion was found to disturb severely the association between mAb 37-7 and hen lysozyme. Moreover, it was demonstrated that, because of the high reproducibility of measurement, the immobilized Fab fragment could detect subtle differences in the surface structure of lysozymes.

Animals↗

PubMed1993

Cycling of two endogenous lysosomal membrane proteins, lamp-2 and acid phosphatase, between the cell surface and lysosomes in cultured rat hepatocytes.

Our previous studies provided evidence that a 107-kDa major lysosomal membrane glycoprotein termed lamp-1 shuttles between lysosomes and the plasma membrane along the endocytic pathway in rat hepatic cells [Furuno et al. (1989) J. Biochem. 106, 708-716; Furuno et al. (1989) J. Biochem. 106, 717-722]. In the present study, we investigated the movement of a 96-kDa major lysosomal membrane glycoprotein, referred to as lamp-2, and lysosomal acid phosphatase (LAP) in the endocytic membrane transport system of cultured rat hepatocytes. Fab' fragments of anti-lamp-2 and anti-LAP antibodies conjugated with horseradish peroxidase (HRP) were used as probes to analyze quantitatively the transport of these two membrane proteins from the cell surface to lysosomes. After the addition of HRP-anti-lamp-2 and anti-LAP Fab' fragments to the culture medium, the delivery of the antibody conjugates to lysosomes was examined by cell fractionation on a Percoll density gradient. The amount of these HRP tracers in the lysosomal fraction became larger as the period of cell incubation was increased. Km values for uptake of HRP-anti-lamp-2, and LAP Fab' fragments were 0.74 and 0.62 microM, respectively, which were comparable to that of HRP-anti-lamp-1 Fab' (0.57 microM). The endocytic process of the two HRP-antibodies continued for an extended period in the cells exposed to the protein synthesis inhibitor, cycloheximide. Furthermore, we measured the transit times of HRP-anti-lamp-1, anti-lamp-2, and anti-LAP Fab' fragments from the cell surface to lysosomes.(ABSTRACT TRUNCATED AT 250 WORDS)

Acid Phosphatase↗

PubMed1992

Isolation and characterization of a novel membrane glycoprotein of 85,000 molecular weight from rat liver lysosomes.

We have purified and characterized a novel glycoprotein (r-lamp-3) with an apparent molecular weight (Mr) of 85,000 from membranes of triton-filled lysosomes (tritosomes) by the use of immunoaffinity chromatography on a column of monoclonal antibody-Sepharose 4B. r-lamp-3 accounted for approximately 4% of the total proteins in tritosomal membranes. The isoelectric point (pI) of r-lamp-3 was 4.5 and it was shifted to 6.5 after neuraminidase treatment with its molecular weight decreased by about 7000. Pulse-chase experiments in cultured rat hepatocytes using [35S]methionine showed that r-lamp-3 was initially synthesized as a 77,000 polypeptide and processed to a mature protein with an Mr of 85,000. Upon treatment with endo-beta-N-acetylglucosaminidase H (Endo H), the precursor and mature forms were converted to 55,000 and 73,000 polypeptides, respectively. From the Mr reduction of the precursor form, we estimated the presence of 10--12 N-linked oligosaccharides/r-lamp-3 polypeptide. The data on enzymatic deglycosylation suggested that the mature form of r-lamp-3 contained the same numbers of high mannose-type and complex-type N-linked oligosaccharide chains.

Animals↗

PubMed1991

Identification and characterization of two distinct kyotorphin-hydrolyzing enzymes in rat brain.

We identified and characterized two kyotorphin-hydrolyzing peptidases (KTPases) in a soluble fraction of rat brain. When the soluble fraction was chromatographed with DEAE-Sephacel, the enzyme activity was resolved into two peaks, which were designated as KTPases I and II in their order of elution. KTPases I and II accounted for 95% and 5% of the KTPase activity in the soluble fraction, respectively. KTPases I and II hydrolyzed kyotorphin with Km values of 22 microM and 110 microM, respectively. By gel filtration, Mr values of KTPases I and II were determined to be 55,000 and 98,000, respectively. Immunological analyses of KTPase II with an anti-enkephalin aminopeptidase antibody indicated that KTPase II was identical to an enkephalin aminopeptidase with Mr = 98,000. However, KTPase I was a novel peptidase responsible for the major kyotorphin-degrading activity in the soluble fraction of rat brain.

Aminopeptidases↗

PubMed1991

Purification, some properties, and tissue distribution of a major lysosome-associated membrane glycoprotein (r-lamp-2) of rat liver.

We previously purified and characterized a major lysosomal membrane glycoprotein (r-lamp-1) from rat liver [Akasaki et al. (1990) Chem. Pharm. Bull. 38, 2766-2770]. The present study describes the purification of another major lysosomal membrane glycoprotein (r-lamp-2) from rat liver and compares the tissue distribution of r-lamp-1 and r-lamp-2 in rats. R-lamp-2 was purified to apparent electrophoretic homogeneity from rat liver by a simple method with a protein yield of approximately 4.0 micrograms/g wet weight of liver. The purification procedure includes: preparation of tritosomal membranes, extraction of tritosomal membranes with Lubrol PX, wheat germ agglutinin (WGA)-Sepharose affinity chromatography, and monoclonal antibody-Sepharose affinity chromatography. R-lamp-2 exhibited an Mr of 96,000 on SDS-PAGE and had an acidic pI of less than 3.5. R-lamp-2 contained 52.3% carbohydrates. Its carbohydrate moieties were composed of numerous sialyl complex type N-linked oligosaccharides and small amounts of O-linked oligosaccharides. Both r-lamp-1 and r-lamp-2 were detected in all rat tissues examined by immunoblot analyses, while their apparent molecular weights differed among the tissues. Immunological quantitative analysis showed that the protein concentrations of r-lamp-2 were consistently lower than those of r-lamp-1 in all the tissues tested. There was a significant correlation with a regression coefficient of 0.86 in the tissue distribution between r-lamp-1 and r-lamp-2. A good correlation was also observed in the tissue distribution between acid phosphatase and r-lamp-2.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1991

An enkephalin-degrading aminopeptidase from rat brain catalyzes the hydrolysis of a neuropeptide, kyotorphin (L-Tyr-L-Arg).

We studied the hydrolysis of a neuropeptide kyotorphin (L-Tyr-L-Arg) by an enkephalin-degrading aminopeptidase purified from cytosol of rat brain in vitro. The purified enzyme was homogeneous as judged by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), gel filtration and isoelectric focusing. The aminopeptidase with an apparent molecular weight (Mr) = 98000 catalyzed the hydrolysis of Leu- and Met-enkephalins with Km values of 125 and 142 microM, respectively. The enzyme activity was inhibited by bestatin, amastatin and puromycin but not by pepstatin, leupeptin and phenylmethanesulfonyl fluoride (PMSF). Kyotorphin was degraded by the aminopeptidase at pH 7.0, and the Vmax and Km values were 9.2 mumol/min/mg protein and 95 microM, respectively. The Km value for kyotorphin was compatible to those for Leu- and Met-enkephalins. Taken together, these results suggest a possible involvement of the enkephalin-degrading aminopeptidase in cytosolic degradation of kyotorphin in neuronal cells of rat brain.

Aminopeptidases↗

PubMed1990

Immunocytochemical study of the surrounding envelope of autophagic vacuoles in cultured rat hepatocytes.

By the use of electron immunoperoxidase cytochemistry at the ultrastructural level, the relationship of the surrounding sac of the autophagic vacuoles to the different cytomembranes was studied. When the endoplasmic reticulum was completely stained for microsomal carboxyesterase E1, the enzyme was not found to be labeled in the developed envelopes forming autophagic vacuoles. The autophagic envelope at the formative stages was also devoid of albumin which intensely stained Golgi cisternae. However, although it was rare, the endoplasmic reticulum showed an electron-lucent region like an early autophagic envelope in its cisternae which was lacking in carboxyesterase E1. In addition, deeply curving swelled cisternae where carboxyesterase E1 was found at the edges were occasionally encountered. These observations suggest that the segregating membranes arise from an endoplasmic reticulum and the structural characteristics of the endoplasmic membranes change at very early stages of formation of autophagic vacuoles. Acid phosphatase, a lysosomal marker enzyme, began to be localized on sections of the double membranes of newly created autophagic vacuoles. The enzyme spread all along the limiting membranes of the autophagic vacuoles, while, at the same time, the double membranes were converted into a single membrane. A lysosomal membrane glycoprotein (LGP107) was also localized on the surrounding envelope of autophagic vacuoles in a fashion similar to that of acid phosphatase. Lysosomal hydrolases seem to play some role in the conversion of double limiting membranes into a single limiting membrane.

Acid Phosphatase↗

PubMed1990

Purification and characterization of a major glycoprotein in rat liver lysosomal membrane.

A major lysosomal membrane glycoprotein (LGP107) which has an apparent molecular weight (Mr) of 107 kilodaltons (kDa) was purified from rat liver by a simple method with a yield of 1 mg/87 g wet weight of liver. The purification procedures include; preparation of tritosomal membranes of triton-filled lysosomes (tritosomes), extraction of tritosomal membranes by Lubrol PX, wheat germ agglutinin (WGA)-Sepharose affinity chromatography, and monoclonal antibody-Sepharose affinity chromatography. The quantitative immunoblot analysis indicated that LGP107 represents 6.2% of the total protein of tritosomal membranes. The isoelectric point of the purified glycoprotein was 2.7, and it moved toward neutral pH after sialidase treatment, with its molecular weight decreased by about 10 kDa. LGP107 contained 52% carbohydrates, and the carbohydrate moiety was compared of Fuc, Man, Gal, GlcNAc and sialic acid in a molar ratio of 7.2:68.2:40.6:63.0:32.3, respectively, indicating that LGP107 was highly glycosylated with N-linked complex-type olgosaccharide chains. Out of the N-linked glycans released from the glycoprotein by hydrazinolysis/N-reacetylation, about 70% was sialylated. Anion exchange and reverse-phase high performance liquid chromatography analysis on the structure of N-glycans revealed that a disialyl biantennary form is a major component in the oligosaccharide chains of LGP107.

Animals↗

PubMed1989

Morphological localization of a major lysosomal membrane glycoprotein in the endocytic membrane system.

We have raised specific polyclonal immunoglobulin G (IgG) against a major lysosomal membrane sialoglycoprotein (LGP107) taken from rat liver and have prepared a conjugate of its Fab' fragment with horseradish peroxidase (HRP-anti LGP107 Fab') as a probe for the subcellular antigen. Electron immunocytochemistry in primary cultured rat hepatocytes showed that LGP107 resided primarily within lysosomes and was associated with luminal amorphous materials as well as limiting membranes. In addition, LGP107 was shown to be substantially distributed throughout the endocytic vacuolar system. The glycoprotein was found clustered in coated pits at the cell surface and localized along the surrounding membranes in endocytic vesicles. When cultured cells were exposed to HRP-anti LGP107 Fab', the antibody which was bound to its antigen within the coated pits was internalized via a system of endocytic vesicles and transported to lysosomes. During 20 min of incubation at 37 degrees C, the HRP tracer appeared at an early stage in small vesicles and moved progressively to larger vesicles, including multivesicular bodies. After 1 h, the tracer could be clearly seen in lysosomes heterogeneous in shape and size. The existence of LGP107 in endocytic compartments and the uptake of anti LGP107 antibody by hepatocytes were not blocked by prior treatment of the cells with cycloheximide and excess amounts of anti LGP107 IgG. These data suggest that LGP107 circulates between the cell surface and lysosomes through the endocytic membrane traffic in hepatocytes.

Animals↗

PubMed1989

Biochemical analysis of the movement of a major lysosomal membrane glycoprotein in the endocytic membrane system.

HRP-anti LGP107Fab' and 125I-anti LGP107IgG were used as probes to study the movement of LGP107 in the endocytic membrane transport system in primary cultured hepatocytes of rats. Following the addition of HRP-anti LGP107Fab' to the culture medium, the transfer of the antibody conjugate from the cell surface of lysosomes was examined by cell fractionation on Percoll density gradients. The HRP tracer showed a bimodal subcellular distribution, in plasma membrane and lysosomal fractions. The amount of HRP found in the lysosomal fractions became larger as the period of cell incubation was increased. The rate of HRP accumulation in lysosomes was 0.13% of the administered load per hour per 10(6) cells. When cells were given 125I-anti LGP107 IgG, the antibody was not stored but was rapidly degraded in the lysosomes. The uptake of 125I-IgG by the cells, which was assessed by measuring the TCA-soluble radiolabeled degradation products released into the medium, increased proportionally to the administered concentration of the antibody and to the incubation time. The rate of uptake of the polyvalent 125I-IgG was comparable to that for the uptake of the monovalent HRP-Fab', and remained unchanged even after long exposure of the cells to a saturating concentration of the polyvalent IgG. This uptake process continued for many hours in the cells exposed to the protein synthesis inhibitor, cycloheximide. These results suggest that there is a continuous circulation of LGP107 between the cell surface and lysosomes in hepatocytes.

Animals↗

PubMed1970

[Carcinoid].

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Carcinoid Tumor↗