Background: Multiple members of the transforming growth factor-β (TGF-β) superfamily have well-established roles in bone homeostasis. Anti-Müllerian hormone (AMH) is a member of TGF-β superfamily of glycoproteins that is responsible for the regression of fetal Müllerian ducts and the transcription inhibition of gonadal steroidogenic enzymes. However, the involvement of AMH in bone remodeling is unknown. Therefore, we investigated whether AMH has an effect on bone cells as other TGF-β superfamily members do. Methods: To identify the roles of AMH in bone cells, we administered AMH during osteoblast and osteoclast differentiation, cultured the cells, and then stained the cultured cells with Alizarin red and tartrate-resistant acid phosphatase, respectively. We analyzed the expression of osteoblast- or osteoclast-related genes using real-time polymerase chain reaction and western blot. Results: AMH does not affect bone morphogenetic protein 2-mediated osteoblast differentiation but inhibits receptor activator of nuclear factor-κB (NF-κB) ligand-induced osteoclast differentiation. The inhibitory effect of AMH on osteoclast differentiation is mediated by IκB-NF-κB signaling. Conclusions AMH negatively regulates osteoclast differentiation without affecting osteoblast differentiation.

Background: Multiple members of the transforming growth factor-β (TGF-β) superfamily have well-established roles in bone homeostasis. Anti-Müllerian hormone (AMH) is a member of TGF-β superfamily of glycoproteins that is responsible for the regression of fetal Müllerian ducts and the transcription inhibition of gonadal steroidogenic enzymes. However, the involvement of AMH in bone remodeling is unknown. Therefore, we investigated whether AMH has an effect on bone cells as other TGF-β superfamily members do. Methods: To identify the roles of AMH in bone cells, we administered AMH during osteoblast and osteoclast differentiation, cultured the cells, and then stained the cultured cells with Alizarin red and tartrate-resistant acid phosphatase, respectively. We analyzed the expression of osteoblast- or osteoclast-related genes using real-time polymerase chain reaction and western blot. Results: AMH does not affect bone morphogenetic protein 2-mediated osteoblast differentiation but inhibits receptor activator of nuclear factor-κB (NF-κB) ligand-induced osteoclast differentiation. The inhibitory effect of AMH on osteoclast differentiation is mediated by IκB-NF-κB signaling. Conclusions AMH negatively regulates osteoclast differentiation without affecting osteoblast differentiation.

Phosphatidylinositol phosphates (PtdInsPs) are ubiquitous membrane phospholipids that play diverse roles in cell growth and differentiation. To clarify the regulation mechanism acting on neurofilament light chain (NF-L) self assembly, we examined the effects of various PtdInsPs on this process. We found that PtdInsPs, including PI(4,5)P2, directly bind to the positively charged Arg54 of murine NF-L, and this binding promotes NF-L self assembly in vitro. Mutant NF-L (R53A/R54A) proteins lacking binding affinity to PtdInsPs did not have the same effect, but the mutant NF-L proteins showed greater self assembly than the wild-type in the absence of any PtdInsP. These results collectively suggest that Arg54 plays a pivotal role in NF-L self assembly by binding with PtdInsPs.
Animals ; Fluorescent Antibody Technique ; Mice ; Mutation/genetics ; Neurofilament Proteins/genetics/*metabolism ; Phosphatidylinositol Phosphates/*metabolism ; Phospholipase C gamma/metabolism ; *Protein Multimerization

PURPOSE: It is difficult to differentiate urothelial tumours of the renal pelvis, invading the renal parenchyma, from renal cell carcinomas, invading the renal pelvis or calyx. The purpose of this study was to assess the differences between the two conditions. MATERIALS AND METHODS: We retrospectively reviewed the medical records, and imaging studies, of 17 patients who underwent nephroureterectomy with bladder cuff excision for urothelial tumours of the renal pelvis, with parenchymal invasion, and of 30 patients who underwent radical nephrectomy for renal cell carcinomas, invading into the renal pelvis or calyx. We assessed the differences in clinical symptoms, urine cytology, intravenous urography, and CT findings between the two conditions. Pearson chi-square tests, with continuity corrections, were performed for statistical analyses. RESULTS: Renal cell carcinomas showed gross hematuria in only 10 cases (33%), positive findings of urine cytology in 1 case of 9 cases (11%). CT scans demonstrated contour bulging in 25 cases (83%), preservation of reniform shape in 5 cases (17%), peripheral location of tumour in 25 cases (83%), and abnormal CT nephogram in 1 cases (3%). In contrast, urothelial tumour of the renal pelvis showed gross hematuria in 13 cases (76%), positive findings of urine cytology in 9 cases of 15 cases (60%). CT scans demonstrated contour bulging in 1 cases (6%), preservation of reniform shape in 16 cases (94%), central location of tumour in all cases (100%), and abnormal CT nephogram in 10 cases (59%). There was no significant difference between renal cell carcinomas and urothelial tumours of the renal pelvis in blood chemistry or IVP. There were no cases of renal cell carcinoma concurrently with bladder tumour, while 2 cases (12%) of urothelial tumour of the renal pelvis had bladder tumours at the same time. CONCLUSIONS: The presence of gross hematuria, positive findings in urine cytology, the presence of bladder tumours, and tumour location, renal contour changes and CT nephogram in CT scans may be helpful in distinguishing both disease entities.
Carcinoma, Renal Cell* ; Chemistry ; Diagnosis, Differential ; Hematuria ; Humans ; Kidney Pelvis* ; Medical Records ; Nephrectomy ; Retrospective Studies ; Tomography, X-Ray Computed ; Urinary Bladder ; Urography

Paragonimiasis is an infection caused by the tematode Paragonimus westermani. Paragonimiasis is endemic in parts of South America, Africa, East and Southest Asia. Human infection occurs by ingestion of raw or incompletely cooked flesh crabs or crayfish infected with metacercaria. Although the lung is the primary site of infection, other organs, notably the brain, may be involved. It rarely affects in abdomen. However, involvement of several intra-abdominal organs has been described. In our knowledge, an ectopic paragonimiasis in prevesical space mimicking urachal cystic mass has not been reported. In this report, we present a case of ectopic paragonimiasis mimicking urachal cystic mass in 66-year-old male.
Abdomen ; Africa ; Aged ; Asia ; Astacoidea ; Brain ; Eating ; Humans ; Lung ; Male ; Paragonimiasis* ; Paragonimus westermani ; South America ; Urachal Cyst*

Growth factor stimulation induces Y783 phosphorylation of phosphoinositide-specific PLC-gamma1, and the subsequent activation of this enzyme in a cellular signaling cascade. Previously, we showed that a double point mutation, Y509A/F510A, of PLC-gamma1, abolished interactions with translational elongation factor 1-alpha. Here, we report that the Y509A/F510A mutant PLC-gamma1 displayed extremely high levels of Y783 phosphorylation and enhanced catalytic activity, compared to wild-type PLC-gamma1, upon treatment of COS7 cells with EGF. In quiescent COS7 cells, the Y509A/F510A mutant PLC-gamma1 exhibited a constitutive hydrolytic activity, whereas the wild-type counterpart displayed a basal level of activity. Upon treatment of COS7 cells with EGF, the Y783F mutation in Y509A/F510A PLC-gamma1 (Y509A/F510A/Y783F triple mutant) cells also led to an enhanced catalytic activity, whereas Y783F mutation alone displayed a basal level of activity. Our results collectively suggest that the Y509A/F510A mutant is more susceptible to receptor tyrosine kinase-induced Y783 phosphorylation than is wild-type PLC-gamma1, but no longer requires Y783 phosphorylation step for the Y509A/F510A mutant PLC-gamma1 activation in vivo.
Amino Acid Substitution/drug effects/*genetics ; Animals ; COS Cells ; Cercopithecus aethiops ; Enzyme Activation/drug effects ; Epidermal Growth Factor/*pharmacology ; Hydrolysis/drug effects ; Mutant Proteins/metabolism ; Phosphatidylinositols/*metabolism ; Phospholipase C gamma/*genetics/metabolism ; Phosphorylation/drug effects ; Phosphotyrosine/*metabolism ; Point Mutation/*genetics ; Rats

Congenital Abnormalities ; Deglutition ; Dentures ; Humans ; Induction Chemotherapy ; Lymph Nodes ; Mouth Neoplasms ; Myocutaneous Flap ; Neck ; Neoplasm Metastasis ; Peplomycin ; Tissue Donors