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Ovarian teratomas are broadly classified histologically into monodermal teratomas (carcinoid tumors, neural tumors, struma ovarii), immature teratomas, and mature cystic teratomas. The most common type among these tumors is mature cystic teratoma, also known as "Dermoid cyst." Cystic teratomas constitute about 20% of ovarian germ cell tumors. The most common site of occurrence is in the ovaries and testes. However, they can rarely be seen in the anterior mediastinum, sacrococcygeal region, or neck. Mature cystic teratoma is always benign with a slow growth rate of 1.8 mm/year; however, in rare circumstances, it can undergo malignant transformation.

Multiple studies have identified some risk factors that have been linked to mature cystic teratomas. They include the following: late menarche with menstrual irregularities, alcohol abuse, history of cystic teratoma in the past, fewer pregnancies, infertility, exercise during adolescence (related to anovulatory menstrual cycles).[3]

The specificity of S-RNase-based self-incompatibility (SI) is controlled by two S-locus genes, the pistil S-RNase gene and the pollen S-locus-F-box gene. S-RNase is synthesized in the transmitting cell; its signal peptide is cleaved off during secretion into the transmitting tract; and the mature "S-RNase", the subject of this study, is taken up by growing pollen tubes via an as-yet unknown mechanism. Upon uptake, S-RNase is sequestered in a vacuolar compartment in both non-self (compatible) and self (incompatible) pollen tubes, and the subsequent disruption of this compartment in incompatible pollen tubes correlates with the onset of the SI response. How the S-RNase-containing compartment is specifically disrupted in incompatible pollen tubes, however, is unknown. Here, we circumvented the uptake step of S-RNase by directly expressing S(2)-RNase, S(3)-RNase and non-glycosylated S(3)-RNase of Petunia inflata, with green fluorescent protein (GFP) fused at the C-terminus of each protein, in self (incompatible) and non-self (compatible) pollen of transgenic plants. We found that none of these ectopically expressed S-RNases affected the viability or the SI behavior of their self or non-self-pollen/pollen tubes. Based on GFP fluorescence of in vitro-germinated pollen tubes, all were sequestered in both self and non-self-pollen tubes. Moreover, the S-RNase-containing compartment was dynamic in living pollen tubes, with movement dependent on the actin-myosin-based molecular motor system. All these results suggest that glycosylation is not required for sequestration of S-RNase expressed in pollen tubes, and that the cytosol of pollen is the site of the cytotoxic action of S-RNase in SI.

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